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<div class="pre-content"><div><div class="bk_prnt"><p class="small">NCBI Bookshelf. A service of the National Library of Medicine, National Institutes of Health.</p><p>Probe Reports from the NIH Molecular Libraries Program [Internet]. Bethesda (MD): National Center for Biotechnology Information (US); 2010-. </p></div><div class="iconblock clearfix whole_rhythm no_top_margin bk_noprnt"><a class="img_link icnblk_img" title="Table of Contents Page" href="/books/n/mlprobe/"><img class="source-thumb" src="/corehtml/pmc/pmcgifs/bookshelf/thumbs/th-mlprobe-lrg.png" alt="Cover of Probe Reports from the NIH Molecular Libraries Program" height="100px" width="80px" /></a><div class="icnblk_cntnt eight_col"><h2>Probe Reports from the NIH Molecular Libraries Program [Internet].</h2><a data-jig="ncbitoggler" href="#__NBK47340_dtls__">Show details</a><div style="display:none" class="ui-widget" id="__NBK47340_dtls__"><div>Bethesda (MD): National Center for Biotechnology Information (US); 2010-.</div></div><div class="half_rhythm"><ul class="inline_list"><li style="margin-right:1em"><a class="bk_cntns" href="/books/n/mlprobe/">Contents</a></li></ul></div><div class="bk_noprnt"><form method="get" action="/books/n/mlprobe/" id="bk_srch"><div class="bk_search"><label for="bk_term" class="offscreen_noflow">Search term</label><input type="text" title="Search this book" id="bk_term" name="term" value="" data-jig="ncbiclearbutton" /> <input type="submit" class="jig-ncbibutton" value="Search this book" submit="false" style="padding: 0.1em 0.4em;" /></div></form></div></div><div class="icnblk_cntnt two_col"><div class="pagination bk_noprnt"><a class="active page_link prev" href="/books/n/mlprobe/ml075/" title="Previous page in this title">&lt; Prev</a><span class="inactive page_link next">Next &gt;</span></div></div></div></div></div>
<div class="main-content lit-style" itemscope="itemscope" itemtype="http://schema.org/CreativeWork"><div class="meta-content fm-sec"><h1 id="_NBK47340_"><span class="title" itemprop="name">Discovery of a Highly Selective <i>in vitro</i> and <i>in
vivo</i> M1 Allosteric Agonist Probe</span></h1><p class="contrib-group"><span itemprop="author">Craig Lindsley</span>, <span itemprop="author">Michelle Lewis</span>, and <span itemprop="author">Dave Weaver</span>.</p><a data-jig="ncbitoggler" href="#__NBK47340_ai__" style="border:0;text-decoration:none">Author Information and Affiliations</a><div style="display:none" class="ui-widget" id="__NBK47340_ai__"><p class="contrib-group"><h4>Authors</h4><span itemprop="author">Craig Lindsley</span>,<sup>1</sup> <span itemprop="author">Michelle Lewis</span>,<sup>2</sup> and <span itemprop="author">Dave Weaver</span><sup>3</sup>.</p><h4>Contact</h4><div class="affiliation"><sup>1</sup> <span class="email-label">Email: </span><a href="mailto:dev@null" data-email="ude.tlibrednav@yelsdnil.giarc" class="oemail">ude.tlibrednav@yelsdnil.giarc</a></div><div class="affiliation"><sup>2</sup> <span class="email-label">Email: </span><a href="mailto:dev@null" data-email="ude.tlibrednav@siwel.ellehcim" class="oemail">ude.tlibrednav@siwel.ellehcim</a></div><div class="affiliation"><sup>3</sup> <span class="email-label">Email: </span><a href="mailto:dev@null" data-email="ude.tlibrednav@revaew.divad" class="oemail">ude.tlibrednav@revaew.divad</a></div></div><p class="small">Received: <span itemprop="datePublished">December 3, 2008</span>; Last Update: <span itemprop="dateModified">October 4, 2010</span>.</p></div><div class="jig-ncbiinpagenav body-content whole_rhythm" data-jigconfig="allHeadingLevels: ['h2'],smoothScroll: false" itemprop="text"><div id="_abs_rndgid_" itemprop="description"><p>Previous attempts to develop compounds that are highly selective for M1 or other specific muscarinic acetylcholine receptor (mAChR) subtypes have failed because of the high conservation of the ACh binding site and difficulty in developing truly specific compounds. Basic and clinical studies suggest that mAChR activation has the potential to be disease modifying, as well as to provide palliative cognitive therapy. Probes developed from these efforts will greatly advance the current state of the art by aiding in the understanding of M1's role in cell-based physiology and may extend the clinical understanding of psychotic and cognitive symptoms associated with neurodegenerative disorders such as Alzheimer's Disease and schizophrenia. This probe report describes ML071 (CID-25010775), a highly selective, potent M1 agonist that activates M1 by virtue of binding at an allosteric site in the third extracellular loop of the M1 receptor. The compound represents a "best in class" probe that provides unprecedented mAChR selectivity, clean ancillary pharmacology, saline solubility, and central penetrance. Furthermore, it can be employed for in vitro and in vivo studies to examine the role of selective M1 receptor activation.</p></div><div class="h2"></div><p><b>Assigned Assay Grant #:</b> X01 MH077606-01</p><p><b>Screening Center Name &#x00026; PI:</b> Vanderbilt Screening Center for GPCRs,
Ion Channels, and Transporters, David Weaver</p><p><b>Chemistry Center Name &#x00026; PI:</b> Vanderbilt Specialized Chemistry Center
for Accelerated Probe Development, Craig Lindsley</p><p><b>Assay Submitter &#x00026; Institution:</b> P. Jeffrey Conn, Vanderbilt
University</p><p><b>PubChem Summary Bioassay Identifier (AID):</b>
<a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1798" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1798</a></p><div id="ml071.s2"><h2 id="_ml071_s2_">Probe Structure &#x00026; Characteristics</h2><p>Ethyl 4-(2-methylbenzamido)ethylamino)piperidine-1-carboxylate hydrochloride</p><div id="ml071.fu1" class="figure"><div class="graphic"><img src="/books/NBK47340/bin/ml071fu1.jpg" alt="Image ml071fu1" /></div></div><div id="ml071.tu1" class="table"><p class="large-table-link" style="display:none"><span class="right"><a href="/books/NBK47340/table/ml071.tu1/?report=objectonly" target="object">View in own window</a></span></p><div class="large_tbl" id="__ml071.tu1_lrgtbl__"><table><thead><tr><th id="hd_h_ml071.tu1_1_1_1_1" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">CID</th><th id="hd_h_ml071.tu1_1_1_1_2" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">Target Name</th><th id="hd_h_ml071.tu1_1_1_1_3" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">IC50/EC50 (nM) [SID,
AID]</th><th id="hd_h_ml071.tu1_1_1_1_4" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">Anti-target Name(s)</th><th id="hd_h_ml071.tu1_1_1_1_5" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">IC50/EC50 (&#x003bc;M)
[SID, AID]</th><th id="hd_h_ml071.tu1_1_1_1_6" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">Selectivity</th><th id="hd_h_ml071.tu1_1_1_1_7" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">Secondary<br /><br />Assay(s) Name:
IC50/EC50</th></tr></thead><tbody><tr><td headers="hd_h_ml071.tu1_1_1_1_1" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">
<b>25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>)</b>
</td><td headers="hd_h_ml071.tu1_1_1_1_2" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">
<b>M1</b>
</td><td headers="hd_h_ml071.tu1_1_1_1_3" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">
<b>198</b>
<br />
<br />
<b>[<a href="https://pubchem.ncbi.nlm.nih.gov/substance/56353039" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">SID-56353039</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/626" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-626</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1488" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1488</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1741" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1741</a>,
<a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1744" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1744</a>]</b>
</td><td headers="hd_h_ml071.tu1_1_1_1_4" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">
<b>M2&#x02013;M5</b>
</td><td headers="hd_h_ml071.tu1_1_1_1_5" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;"><b>&#x0003e;30</b>
&#x003bc;<b>M</b><br /><br /><b>[<a href="https://pubchem.ncbi.nlm.nih.gov/substance/56353039" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">SID-56353039</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/626" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-626</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1488" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1488</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1741" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1741</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1744" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1744</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1470" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1470</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1767" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1767</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1764" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1764</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1757" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1757</a>,
<a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1508" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1508</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1788" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1788</a>]</b></td><td headers="hd_h_ml071.tu1_1_1_1_6" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">
<b>&#x0003e;263-fold</b>
</td><td headers="hd_h_ml071.tu1_1_1_1_7" rowspan="1" colspan="1" style="text-align:center;vertical-align:top;">
<b>M1 Y381A 379 nM [<a href="https://pubchem.ncbi.nlm.nih.gov/substance/56353039" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">SID-56353039</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1743" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1743</a>]</b>
</td></tr></tbody></table></div></div></div><div id="ml071.s3"><h2 id="_ml071_s3_">Recommendations for the scientific use of this probe</h2><p>This probe can be used for both <i>in vitro</i> and <i>in
vivo</i> to study the role of selective M1 receptor activation. The
compound possesses unprecedented selectivity versus M2&#x02013;M5 and against a
large panel of GPCRs, ion channels and transporters. Moreover, the probe is
centrally penetrant and soluble in saline (&#x0003e;25 mg/mL).</p><div id="ml071.s4"><h3>Specific Aim</h3><p>To identify small molecule agonists of M1 muscarinic receptor that are cell
permeable, exhibit submicromolar potency, and show greater than 10 fold
selectivity over other muscarinic family members M2, M3, M4 and M5. This probe
report describes a potent, highly selective M1 allosteric agonist (CID 25010775
(<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>), <a href="https://pubchem.ncbi.nlm.nih.gov/substance/56353039" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">SID-56353039</a>) that activates M1 by virtue of binding at an allosteric
site in the third extracellular loop of the M1 receptor. The probe is
&#x02018;best in class&#x02019; providing unprecedented mAChR
selectivity, clean ancillary pharmacology, soluble in saline (~25 mg/mL) and
centrally penetrant.</p></div><div id="ml071.s5"><h3>Significance</h3><p>Previous attempts to develop compounds that are highly selective for M1 or other
specific mAChR subtypes have failed because of the high conservation of the Ach
binding site and difficulty in developing truly specific compounds (<a class="bk_pop" href="#ml071.r2">Bonner et al. 1997</a>, <a class="bk_pop" href="#ml071.r3">1998</a>; <a class="bk_pop" href="#ml071.r7">Felder et al. 2000</a>; <a class="bk_pop" href="#ml071.r4">Bymaster et al. 2003</a>). The lack of highly selective
compounds has made it impossible to definitively determine the behavioral and
clinical effects of these receptors. In numerous Phase II and III clinical
trails, pan-mAChR agonists were shown to improve cognitive performance in AD
patients, but the GI-and/or cardiovascular side effects, resulting from
activation of peripheral mAChRs, were deemed intolerable and the trials were
discontinued (Eglen et al. 2001; Tarsy et al. 2006). Importantly, several
pan-mAChR agonists demonstrated decline of A&#x003b2;42 in the cerebral
spinal fluid of AD patients, suggesting that mAChR activation has the potential
to be disease modifying as well as providing palliative cognitive therapy (<a class="bk_pop" href="#ml071.r1">Bodick et al. 1997</a>). More recent
studies in 3xTg-AD mice further support a disease modifying role for mAChR
activation, and several Ph III trials demonstrated that mAChR activation lowered
A&#x003b2;42 in patients (<a class="bk_pop" href="#ml071.r5">Caccamo et
al. 2006</a>). Interestingly, the M1/M4 preferring xanomeline, in
addition to improving cognitive performance, had robust therapeutic effects on
the psychotic symptoms and behavioral disturbances associated with AD and
recently published clinical trial data indicates efficacy in schizophrenic
patients (<a class="bk_pop" href="#ml071.r1">Bodick et al. 1997</a>; <a class="bk_pop" href="#ml071.r10">Shekhar et al. 2008</a>). Probes
developed from these efforts will greatly advance the current state of the art
by aiding in the understanding of M1&#x02019;s role in cell-based physiology
and may extend the clinical understanding of psychotic and cognitive symptoms
associated with neurodegenerative disorders like Alzheimer&#x02019;s Disease
and schizophrenia.</p></div><div id="ml071.s6"><h3>Rationale</h3><p>In recent years, major advances have been made in the discovery of highly
selective agonists of other G protein-coupled receptors (GPCRs) that act at an
allosteric site rather than the orthosteric binding site (<a class="bk_pop" href="#ml071.r9">May et al. 2003</a>). By screening for compounds that act
at an allosteric site on the receptor, it is anticipated that compounds that
selectively activate M1 versus the other muscarinic subtypes may be identified.
While allosteric M1 agonists have been identified, AC-42 and TBPB, they both
suffer from undesirable ancillary pharmacology, poor physicochemical properties,
poor pharmacokinetics and/or limited CNS penetration (<a class="bk_pop" href="#ml071.r11">Spalding et al. 2002</a>; <a class="bk_pop" href="#ml071.r8">Jones et al. 2008</a>). Thus, to truly enable the
biomedical community to dissect the relative contributions of selective M1
activation in preclinical models of AD and schizophrenia and to understand the
role of M1 in the pronounced efficacy of the M1/M4 preferring xanomeline,
improved M1 probes are required.</p><p><b><i>Screening center information</i></b></p><p>Assay Implementation and Screening</p><p><b>PubChem Bioassay Name:</b> Discovery of novel allosteric modulators of the M1 muscarinic
receptor: Agonist</p><p><b>List of PubChem bioassay identifiers generated for this screening
project (AIDS):</b>
<a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/626" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-626</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1488" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1488</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1741" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1741</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1508" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1508</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1470" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1470</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1744" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1744</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1767" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1767</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1764" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1764</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1757" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1757</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1743" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1743</a>, <a href="https://pubchem.ncbi.nlm.nih.gov/bioassay/1788" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">AID-1788</a>.</p></div></div><div id="ml071.s11"><h2 id="_ml071_s11_">PubChem Primary Assay Description</h2><ol><li class="half_rhythm"><div>Hamster Ovary (CHO) cells containing M1 receptor (ATCC#CRL-1985)
were plated at 10,000 cells/well in assay media (F12 (Ham), 10%
FBS, 2 millimolar GlutaMAX (Invitrogen), 20mM HEPES) in 384 well plates.</div></li><li class="half_rhythm"><div>The plates were incubated overnight at 37 degrees C in 5%
CO2.</div></li><li class="half_rhythm"><div>Media was removed and assay buffer (Hanks Balanced Salt Solution, 20
millimolar HEPES, 2.5 millimolar Probenecid, pH 7.4) containing 4.0
micromolar Fluo4-AM dye (Invitrogen) was added.</div></li><li class="half_rhythm"><div>Cells were incubated for 45 minutes (37 degrees C, 5% CO2) for
dye loading.</div></li><li class="half_rhythm"><div>Cell plates were loaded into the Hamamatsu FDSS equipped with 480 nanometer
excitation and 540 nanometer emission filters.</div></li><li class="half_rhythm"><div>10 micromolar test compound in assay buffer + 0.1%
DMSO was added at 5 seconds; simultaneously, the plate was kinetically
imaged.</div></li><li class="half_rhythm"><div>Subsequently, 8 nanomolar acetylcholine (EC80) in assay buffer was added at
197 seconds and imaging continued for a total of 4 minutes acquisition
time.</div></li><li class="half_rhythm"><div>0.1% DMSO, compound vehicle, and 80nM acetylcholine (ECMAX) were
added to each plate as controls.</div></li><li class="half_rhythm"><div>Compounds that stimulated an increase in intracellular calcium upon their
addition deviating by more than three standard deviations from the test
populations were identified as &#x0201c;hits&#x0201d;.</div></li></ol><div id="ml071.s12"><h3>Summary of Screen</h3><p>For the discovery of novel allosteric agonists of the M1 muscarinic receptor, we
completed the primary screen using a real-time cell-based assay against the full
65K library. The assay performed very well (Z&#x02032; averaged 0.7) and we
identified approximately 2000 putative agonist primary hits. The compounds
clustered nicely into different structural classes with multiple representative
analogs in each cluster. The agonist compounds were chosen as the focus of this
probe effort, but we previously filed a probe report for the first truly
selective small molecule M1 antagonist, <a href="https://pubchem.ncbi.nlm.nih.gov/substance/56373925" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">SID-56373925</a>.</p><p>For the confirmation screen, 1666 agonist hits were reordered from Biofocus-DPI.
The compounds were tested in duplicate against M1/CHO cells, and in parallel,
counter screened against M4/Gqi5 CHO cells. Compounds showing initial
selectivity for M1 over M4 were tested in triplicate in a 10 point dose-response
series against the muscarinic panel (M1&#x02013;M5). Compounds showing
selectivity for M1 were then tested as a concentration series in the presence of
atropine. Pubchem CID 644390 and CID 647412 were selective (&#x0003e;50-fold) for
M1 vs. M4 with M1 EC<sub>50</sub>s from the DPI DMSO stock of ~ 1 &#x003bc;M
(<a class="figpopup" href="/books/NBK47340/figure/ml071.f1/?report=objectonly" target="object" rid-figpopup="figml071f1" rid-ob="figobml071f1">Figure 1</a>) and sensitive to block
by atropine.</p><div class="iconblock whole_rhythm clearfix ten_col fig" id="figml071f1" co-legend-rid="figlgndml071f1"><a href="/books/NBK47340/figure/ml071.f1/?report=objectonly" target="object" title="Figure 1" class="img_link icnblk_img figpopup" rid-figpopup="figml071f1" rid-ob="figobml071f1"><img class="small-thumb" src="/books/NBK47340/bin/ml071f1.gif" src-large="/books/NBK47340/bin/ml071f1.jpg" alt="Figure 1. M1 vs. M4 selective Agonist Leads from the HTS." /></a><div class="icnblk_cntnt" id="figlgndml071f1"><h4 id="ml071.f1"><a href="/books/NBK47340/figure/ml071.f1/?report=objectonly" target="object" rid-ob="figobml071f1">Figure 1</a></h4><p class="float-caption no_bottom_margin">M1 vs. M4 selective Agonist Leads from the HTS. </p></div></div><p>We then resynthesized the two HTS leads to confirm structure and activity (<a class="figpopup" href="/books/NBK47340/figure/ml071.f11/?report=objectonly" target="object" rid-figpopup="figml071f11" rid-ob="figobml071f11">Scheme 1</a>). In the event, commercial
mono- <i>N</i>-Boc diaminoethane was acylated with either
2-chlorobenzoyl chloride (<b>2</b>) or 2-thienyl acyl chloride
(<b>3</b>) to deliver <b>4</b> and <b>5</b>, respectively.
The Boc group was removed by exposure to 4N HCl/dioxane to provide the
corresponding HCl salts <b>6</b> and <b>7</b>. Finally, a reductive
amination sequence employing ethyl-4-oxopiperidine-1-carboxylate (8) with a
polymer-supported hydride delivered the original HTS leads, CID 644390 and CID
647412 in overall yields for the three step sequence in excess of
70%.</p><div class="iconblock whole_rhythm clearfix ten_col fig" id="figml071f11" co-legend-rid="figlgndml071f11"><a href="/books/NBK47340/figure/ml071.f11/?report=objectonly" target="object" title="Scheme 1" class="img_link icnblk_img figpopup" rid-figpopup="figml071f11" rid-ob="figobml071f11"><img class="small-thumb" src="/books/NBK47340/bin/ml071f11.gif" src-large="/books/NBK47340/bin/ml071f11.jpg" alt="Scheme 1. Resynthesis of M1 vs. M4 selective Agonist Leads from the HTS; 70% overall yield." /></a><div class="icnblk_cntnt" id="figlgndml071f11"><h4 id="ml071.f11"><a href="/books/NBK47340/figure/ml071.f11/?report=objectonly" target="object" rid-ob="figobml071f11">Scheme 1</a></h4><p class="float-caption no_bottom_margin">Resynthesis of M1 vs. M4 selective Agonist Leads from the HTS;
70% overall yield. </p></div></div><p>The resynthesized CID 644390 and CID 647412 confirmed, with M1 EC<sub>50</sub>s
of 804 nM and 1.74 &#x003bc;M, respectively. Importantly, both compounds
proved to be highly selective versus M2&#x02013;M5, affording no activation
at concentrations exceeding 50 &#x003bc;M (<a class="figpopup" href="/books/NBK47340/figure/ml071.f2/?report=objectonly" target="object" rid-figpopup="figml071f2" rid-ob="figobml071f2">Figure 2</a>). Based on this unprecedented mAChR
selectivity, we assumed these ligands must be binding at an allosteric
sitetoelicit receptor activation. Competition binding studies with the
orthosteric antagonist [<sup>3</sup>H]-NMS demonstrated
that CID 644390 (<a href="https://pubchem.ncbi.nlm.nih.gov/substance/842134" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">SID-842134</a>) and CID 647412 (<a href="https://pubchem.ncbi.nlm.nih.gov/substance/845074" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">SID-845074</a>) displace the
radioligand only at very high concentrations, suggesting they do in fact bind at
an allosteric site (<a class="figpopup" href="/books/NBK47340/figure/ml071.f3/?report=objectonly" target="object" rid-figpopup="figml071f3" rid-ob="figobml071f3">Figure 3</a>).
However, these initial hits do not meet MLPCN probe criteria, so we initiated a
chemical lead optimization campaign to develop a selective M1 allosteric agonist
that meets MLPCN criteria.</p><div class="iconblock whole_rhythm clearfix ten_col fig" id="figml071f2" co-legend-rid="figlgndml071f2"><a href="/books/NBK47340/figure/ml071.f2/?report=objectonly" target="object" title="Figure 2" class="img_link icnblk_img figpopup" rid-figpopup="figml071f2" rid-ob="figobml071f2"><img class="small-thumb" src="/books/NBK47340/bin/ml071f2.gif" src-large="/books/NBK47340/bin/ml071f2.jpg" alt="Figure 2. In vitro pharmacological profile of resynthesized CID 644390 and CID 647412 on M1&#x02013;M5." /></a><div class="icnblk_cntnt" id="figlgndml071f2"><h4 id="ml071.f2"><a href="/books/NBK47340/figure/ml071.f2/?report=objectonly" target="object" rid-ob="figobml071f2">Figure 2</a></h4><p class="float-caption no_bottom_margin">In vitro pharmacological profile of resynthesized CID 644390 and CID
647412 on M1&#x02013;M5. </p></div></div><div class="iconblock whole_rhythm clearfix ten_col fig" id="figml071f3" co-legend-rid="figlgndml071f3"><a href="/books/NBK47340/figure/ml071.f3/?report=objectonly" target="object" title="Figure 3" class="img_link icnblk_img figpopup" rid-figpopup="figml071f3" rid-ob="figobml071f3"><img class="small-thumb" src="/books/NBK47340/bin/ml071f3.gif" src-large="/books/NBK47340/bin/ml071f3.jpg" alt="Figure 3. Competition Binding with [3H]-NMS." /></a><div class="icnblk_cntnt" id="figlgndml071f3"><h4 id="ml071.f3"><a href="/books/NBK47340/figure/ml071.f3/?report=objectonly" target="object" rid-ob="figobml071f3">Figure 3</a></h4><p class="float-caption no_bottom_margin">Competition Binding with
[<sup>3</sup>H]-NMS. </p></div></div></div></div><div id="ml071.s13"><h2 id="_ml071_s13_">Probe Chemical Lead Optimization Strategy</h2><p>We employed an iterative parallel synthesis approach for the optimization of CID
644390 and CID 647412, as the scaffolds were modular and readily amenable to this
approach. We simultaneously investigated three areas of the scaffold (<a class="figpopup" href="/books/NBK47340/figure/ml071.f4/?report=objectonly" target="object" rid-figpopup="figml071f4" rid-ob="figobml071f4">Figure 4</a>) employing the synthetic route
depicted in <a class="figpopup" href="/books/NBK47340/figure/ml071.f11/?report=objectonly" target="object" rid-figpopup="figml071f11" rid-ob="figobml071f11">Scheme 1</a>, and quickly
noticed (<a class="figpopup" href="/books/NBK47340/table/ml071.t1/?report=objectonly" target="object" rid-figpopup="figml071t1" rid-ob="figobml071t1">Table 1</a>), that responsive SAR
was only observed for the amide moiety (blue). No modifications to the linker region
(yellow) were tolerated, and this included substitutions along the ethyl chain,
capping either terminal nitrogen with a methyl, or homologation of the linker.
Similar flat SAR was observed for the ethyl carbamate moiety (green). No
alternatives (amides, alkyl/phenyl or differen carbamates) were tolerated. Of 40
analogs prepared, only six (15%) displayed any measurable M1 activity.
However, the six active compounds all possessed sub-micromolar EC<sub>50</sub>s at
M1 (152 nM to 459 nM), and all were completely selective versus M2&#x02013;M5
(EC<sub>50</sub>s &#x0003e;50 &#x003bc;M). Thus, all six met the minimum
criteria for an MLPCN probe. We then counter-screened the six compounds versus D2 as
a mean to distinguish the probe candidates, as activity at D2 would greatly diminish
the value of an M1 probe to explore the role of selective M1 activation in
modulating the pathophysiology of schizophrenia. This counter-screen eliminated four
potential probe compounds (low micromolar D2 IC<sub>50</sub>s) and left CID 650889
and CID 25010776 as contenders (D2 IC<sub>50</sub>s &#x0003e;10 &#x003bc;M). The
two potential probes were then resynthesized and screened as the corresponding HCl
salts 650889 (25010774) and 25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>). After completing n=3 CRCs
for the potential probes, the M1 EC<sub>50</sub>s for CID 25010774 and CID 25010775
(<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>) were 152&#x000b1;8.4 nM (85.1&#x000b1;3.3% ACh Max) and
198&#x000b1;13.2 nM (80.52&#x000b1;7.6% ACh Max) with complete
selectivity versus M2&#x02013;M5 (<a class="figpopup" href="/books/NBK47340/figure/ml071.f5/?report=objectonly" target="object" rid-figpopup="figml071f5" rid-ob="figobml071f5">Figure
5a</a>). To confirm that these compounds are indeed allosteric agonists, we
evaluated them on a Y381A mutant M1 cell line. Allosteric agonists of M1 can be
differentiated from orthosteric agonists by their ability to activate the receptor
in which there is a single point mutation (Y381A) in the orthosteric binding site
that renders the receptor insensitive to acetylcholine or orthosteric agonists. As
shown in <a class="figpopup" href="/books/NBK47340/figure/ml071.f5/?report=objectonly" target="object" rid-figpopup="figml071f5" rid-ob="figobml071f5">Figure 5b</a>, the Y381A mutation
causes three order of magnitude right-shift in the ACh CRC and TBPB, the
prototypical M1 allosteric agonist, retains some efficacy on this line. In contrast,
the initial HTS leads (CID 644390 and CID 647412) and the two probe candidates (CID
25010774 and CID 25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>)) remain fully efficacious on this mutant line. In
fact, the EC<sub>50</sub>s for CID 650889 and CID 25010776 shift less than 2-fold
(Y381A M1 EC<sub>50</sub>s = 304&#x000b1;56 nM and
379&#x000b1;91 nM, respectively). These data, coupled with competition binding
studies with [<sup>3</sup>H]-NMS (<a class="figpopup" href="/books/NBK47340/figure/ml071.f6/?report=objectonly" target="object" rid-figpopup="figml071f6" rid-ob="figobml071f6">Figure 6</a>), clearly indicate that these new M1 agonists
activate the receptor through binding at an allosteric site.</p><div class="iconblock whole_rhythm clearfix ten_col fig" id="figml071f4" co-legend-rid="figlgndml071f4"><a href="/books/NBK47340/figure/ml071.f4/?report=objectonly" target="object" title="Figure 4" class="img_link icnblk_img figpopup" rid-figpopup="figml071f4" rid-ob="figobml071f4"><img class="small-thumb" src="/books/NBK47340/bin/ml071f4.gif" src-large="/books/NBK47340/bin/ml071f4.jpg" alt="Figure 4. Chemical Optimization Plan for CID 644390 and CID 647412." /></a><div class="icnblk_cntnt" id="figlgndml071f4"><h4 id="ml071.f4"><a href="/books/NBK47340/figure/ml071.f4/?report=objectonly" target="object" rid-ob="figobml071f4">Figure 4</a></h4><p class="float-caption no_bottom_margin">Chemical Optimization Plan for CID 644390 and CID 647412. </p></div></div><div class="iconblock whole_rhythm clearfix ten_col table-wrap" id="figml071t1"><a href="/books/NBK47340/table/ml071.t1/?report=objectonly" target="object" title="Table 1" class="img_link icnblk_img figpopup" rid-figpopup="figml071t1" rid-ob="figobml071t1"><img class="small-thumb" src="/books/NBK47340/table/ml071.t1/?report=thumb" src-large="/books/NBK47340/table/ml071.t1/?report=previmg" alt="Table 1. Structure-Activity Relationships for Analogs of CID 644390 and CID 647412." /></a><div class="icnblk_cntnt"><h4 id="ml071.t1"><a href="/books/NBK47340/table/ml071.t1/?report=objectonly" target="object" rid-ob="figobml071t1">Table 1</a></h4><p class="float-caption no_bottom_margin">Structure-Activity Relationships for Analogs of CID 644390 and CID
647412. </p></div></div><div class="iconblock whole_rhythm clearfix ten_col fig" id="figml071f5" co-legend-rid="figlgndml071f5"><a href="/books/NBK47340/figure/ml071.f5/?report=objectonly" target="object" title="Figure 5" class="img_link icnblk_img figpopup" rid-figpopup="figml071f5" rid-ob="figobml071f5"><img class="small-thumb" src="/books/NBK47340/bin/ml071f5.gif" src-large="/books/NBK47340/bin/ml071f5.jpg" alt="Figure 5. A) Full CRCs for CID 25010774 and CID 25010775 for wt M1&#x02013;M5; B) CRCs for TBPB, ACh, the initial HTS leads CID 644390 and CID 647412 and the probe candidates CID 25010774 and CID 25010775." /></a><div class="icnblk_cntnt" id="figlgndml071f5"><h4 id="ml071.f5"><a href="/books/NBK47340/figure/ml071.f5/?report=objectonly" target="object" rid-ob="figobml071f5">Figure 5</a></h4><p class="float-caption no_bottom_margin">A) Full CRCs for CID 25010774 and CID 25010775 for wt M1&#x02013;M5;
B) CRCs for TBPB, ACh, the initial HTS leads CID 644390 and CID 647412 and
the probe candidates CID 25010774 and CID 25010775. </p></div></div><div class="iconblock whole_rhythm clearfix ten_col fig" id="figml071f6" co-legend-rid="figlgndml071f6"><a href="/books/NBK47340/figure/ml071.f6/?report=objectonly" target="object" title="Figure 6" class="img_link icnblk_img figpopup" rid-figpopup="figml071f6" rid-ob="figobml071f6"><img class="small-thumb" src="/books/NBK47340/bin/ml071f6.gif" src-large="/books/NBK47340/bin/ml071f6.jpg" alt="Figure 6. Competition [3H]-NMS binding for the initial HTS leads CID 644390 and CID 647412 and the probe candidates CID 25010774 and CID 25010775 relative to the orthosteric antagonist atropine." /></a><div class="icnblk_cntnt" id="figlgndml071f6"><h4 id="ml071.f6"><a href="/books/NBK47340/figure/ml071.f6/?report=objectonly" target="object" rid-ob="figobml071f6">Figure 6</a></h4><p class="float-caption no_bottom_margin">Competition [<sup>3</sup>H]-NMS binding for the
initial HTS leads CID 644390 and CID 647412 and the probe candidates CID
25010774 and CID 25010775 relative to the orthosteric antagonist
atropine. </p></div></div><p>A major liability with TBPB, the leading allosteric M1 agonist in the literature to
date, is the fact that TBPB is a pan-mAChR antagonist at higher concentrations at
M2&#x02013;M5. This undesired ancillary pharmacology greatly limits the utility
of TBPB to cleanly dissect the role of selective M1 activation <i>in
vitro</i> and <i>in vivo</i>. Gratifyingly (<a class="figpopup" href="/books/NBK47340/figure/ml071.f7/?report=objectonly" target="object" rid-figpopup="figml071f7" rid-ob="figobml071f7">Figure 7</a>), the initial HTS leads (CID 644390 and CID
647412) and the two probe candidates (CID 25010774 and CID 25010776) show no
significant antagonism of M2&#x02013;M5 and further distinguish themselves as
superior M1 allosteric agonist probes.</p><div class="iconblock whole_rhythm clearfix ten_col fig" id="figml071f7" co-legend-rid="figlgndml071f7"><a href="/books/NBK47340/figure/ml071.f7/?report=objectonly" target="object" title="Figure 7" class="img_link icnblk_img figpopup" rid-figpopup="figml071f7" rid-ob="figobml071f7"><img class="small-thumb" src="/books/NBK47340/bin/ml071f7.gif" src-large="/books/NBK47340/bin/ml071f7.jpg" alt="Figure 7. Functional antagonism comparison of TBPB and for the initial HTS leads CID 644390 and CID 647412 and the probe candidates CID 25010774 and CID 25010775." /></a><div class="icnblk_cntnt" id="figlgndml071f7"><h4 id="ml071.f7"><a href="/books/NBK47340/figure/ml071.f7/?report=objectonly" target="object" rid-ob="figobml071f7">Figure 7</a></h4><p class="float-caption no_bottom_margin">Functional antagonism comparison of TBPB and for the initial HTS leads
CID 644390 and CID 647412 and the probe candidates CID 25010774 and CID
25010775. </p></div></div><p>In parallel, to further confirm that the two probe candidates (CID 25010774 and CID
25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>)) are indeed activating M1 at an allosteric site, we evaluated both
probe candidates against a mutant line we had in house targeting the third
extracellular loop (e3) that is far removed from the orthosteric binding site. A
(K392D/E397V/E410H) triple mutant abolishes the ability of the two probe candidates
(CID 25010774 and CID 25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>)) to activate M1 (<a class="figpopup" href="/books/NBK47340/figure/ml071.f8/?report=objectonly" target="object" rid-figpopup="figml071f8" rid-ob="figobml071f8">Figure 8</a>). Evaluation of the three individual single point
mutants demonstrated that the E401H is critical for M1 activation with the two probe
candidates (CID 25010774 and CID 25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>)), suggesting they bind to the e3
loop of M1, far removed from the orthosteric binding site.</p><div class="iconblock whole_rhythm clearfix ten_col fig" id="figml071f8" co-legend-rid="figlgndml071f8"><a href="/books/NBK47340/figure/ml071.f8/?report=objectonly" target="object" title="Figure 8" class="img_link icnblk_img figpopup" rid-figpopup="figml071f8" rid-ob="figobml071f8"><img class="small-thumb" src="/books/NBK47340/bin/ml071f8.gif" src-large="/books/NBK47340/bin/ml071f8.jpg" alt="Figure 8. Further data with an M1 triple mutant (K392D/E397V/E401H) for the probe candidates CID 25010774 and CID 25010775, and identification of a lone single point mutant (E401H) that diminishes M1 activation." /></a><div class="icnblk_cntnt" id="figlgndml071f8"><h4 id="ml071.f8"><a href="/books/NBK47340/figure/ml071.f8/?report=objectonly" target="object" rid-ob="figobml071f8">Figure 8</a></h4><p class="float-caption no_bottom_margin">Further data with an M1 triple mutant (K392D/E397V/E401H) for the probe
candidates CID 25010774 and CID 25010775, and identification of a lone
single point mutant (E401H) that diminishes M1 activation. </p></div></div><p>At this point, the Lead Profiling Screen (68 GPCRs, ion channels and transporters)
from MDS Pharma was performed on the two probe candidates (CID 25010774 and CID
25010776) to attempt to distinguish which would be promoted to probe status. CID
25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>) (<a href="https://pubchem.ncbi.nlm.nih.gov/substance/56353039" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">SID-56353039</a>) possessed superior ancillary profile to both TBPB
and CID 25010774 (<a class="figpopup" href="/books/NBK47340/table/ml071.f9/?report=objectonly" target="object" rid-figpopup="figml071f9" rid-ob="figobml071f9">Figure 9</a>), with only
three activities &#x0003e;50% at 10 &#x003bc;M, and was thus declared
an MLPCN probe. CID 25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>) has the following IUPAC nomenclature: ethyl
4-(2-methylbenzamido)ethylamino) piperidine-1-carboxylate.</p><div class="iconblock whole_rhythm clearfix ten_col table-wrap" id="figml071f9"><a href="/books/NBK47340/table/ml071.f9/?report=objectonly" target="object" title="Figure 9" class="img_link icnblk_img figpopup" rid-figpopup="figml071f9" rid-ob="figobml071f9"><img class="small-thumb" src="/books/NBK47340/table/ml071.f9/?report=thumb" src-large="/books/NBK47340/table/ml071.f9/?report=previmg" alt="Figure 9. MDS Pharma Lead Profiling Screen of 68 GPCRs, ion channels and transporters against CID 25010775 (SID-56353039) at a concentration of 10 &#x003bc;M." /></a><div class="icnblk_cntnt"><h4 id="ml071.f9"><a href="/books/NBK47340/table/ml071.f9/?report=objectonly" target="object" rid-ob="figobml071f9">Figure 9</a></h4><p class="float-caption no_bottom_margin">MDS Pharma Lead Profiling Screen of 68 GPCRs, ion channels and transporters against CID 25010775 (SID-56353039) at a concentration of 10 &#x003bc;M. </p></div></div><div id="ml071.fu2" class="figure bk_fig"><div class="graphic"><img src="/books/NBK47340/bin/ml071fu8.jpg" alt="CID 25010776 A Best-in-Class M1 allosteric agonist probe." /></div><h3><span class="title">CID 25010776 A Best-in-Class M1 allosteric agonist probe</span></h3></div><p>Finally, a brain/plasma study was conducted to determine if our M1 allosteric agonist
probe (CID 25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>)) was centrally penetrant after systemic dosing, as this
would add significant value to the probe for the biomedical research community. When
converted to the mono- HCl salt, CID 25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>) displayed excellent solubility
across pharmaceutically acceptable vehicles, as well as DMSO (&#x0003e; 100 mM) and
water (homogeneous solutions up to 25 mg/mL). For the brain/plasma study, CID
25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>) (<a href="https://pubchem.ncbi.nlm.nih.gov/substance/56353039" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubchem">SID-56353039</a>) as the mono-HCl salt, was dosed in water at 10 mg/kg
i.p. to Sprauge-Dawley rats (<a class="figpopup" href="/books/NBK47340/figure/ml071.f10/?report=objectonly" target="object" rid-figpopup="figml071f10" rid-ob="figobml071f10">Figure 10</a>).
A brain/plasma ratio of 4.2 was observed, with the compound preferentially
portioning into the brain. This is an excellent profile for a CNS agent, with brain
levels in the &#x003bc;M range for up to 5 hours post dose - &#x0003e;8-fold
above the EC<sub>50</sub> for M1 activation. Importantly, the animals were closely
monitored, and were healthy, with no signs of classical pan-mAChR activation (SLUD
&#x02013; salivation, lacrimation, urination and defecation) indicating that the
in vitro mAChR selectivity profile was mirrored in vivo. Thus, CID 25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>)
has utility as both an <i>in vitro</i> and <i>in vivo</i> probe
for selective M1 activation by an allosteric mechanism.</p><div class="iconblock whole_rhythm clearfix ten_col fig" id="figml071f10" co-legend-rid="figlgndml071f10"><a href="/books/NBK47340/figure/ml071.f10/?report=objectonly" target="object" title="Figure 10" class="img_link icnblk_img figpopup" rid-figpopup="figml071f10" rid-ob="figobml071f10"><img class="small-thumb" src="/books/NBK47340/bin/ml071f10.gif" src-large="/books/NBK47340/bin/ml071f10.jpg" alt="Figure 10. Brain/plasma study with SID-56353039." /></a><div class="icnblk_cntnt" id="figlgndml071f10"><h4 id="ml071.f10"><a href="/books/NBK47340/figure/ml071.f10/?report=objectonly" target="object" rid-ob="figobml071f10">Figure 10</a></h4><p class="float-caption no_bottom_margin">Brain/plasma study with SID-56353039. </p></div></div><p><a class="figpopup" href="/books/NBK47340/figure/ml071.f12/?report=objectonly" target="object" rid-figpopup="figml071f12" rid-ob="figobml071f12">Scheme 2</a> below highlights the optimized
route to prepare CID 25010776 as the mono-HCl salt CID 25010775 (<a href="/pcsubstance/?term=ML071[synonym]" ref="pagearea=body&amp;targetsite=entrez&amp;targetcat=term&amp;targettype=pubchem">ML071</a>) in
82.5% overall yield. All of the reagents are commercially available from
Aldrich Chemical company. <b>MLS#s:</b> MLS002279948,
MLS002279949, MLS002279950, MLS002279951, MLS002279952, MLS002279953</p><div class="iconblock whole_rhythm clearfix ten_col fig" id="figml071f12" co-legend-rid="figlgndml071f12"><a href="/books/NBK47340/figure/ml071.f12/?report=objectonly" target="object" title="Scheme 2" class="img_link icnblk_img figpopup" rid-figpopup="figml071f12" rid-ob="figobml071f12"><img class="small-thumb" src="/books/NBK47340/bin/ml071f12.gif" src-large="/books/NBK47340/bin/ml071f12.jpg" alt="Scheme 2. Optimized synthesis of CID 25010776 as free base and mono-HCl salt, 25010775: overall yield of 82.5%." /></a><div class="icnblk_cntnt" id="figlgndml071f12"><h4 id="ml071.f12"><a href="/books/NBK47340/figure/ml071.f12/?report=objectonly" target="object" rid-ob="figobml071f12">Scheme 2</a></h4><p class="float-caption no_bottom_margin">Optimized synthesis of CID 25010776 as free base and mono-HCl salt,
25010775: overall yield of 82.5%. </p></div></div></div><div id="ml071.rl1"><h2 id="_ml071_rl1_">Bibliography</h2><ol><li><div class="bk_ref" id="ml071.r1">Bodick NC, Ofen WW, Levey AI, Cutler NR, Gauthier SG, Satlin A, Shannon HE, Tollefson GD, Rasmussen K, Bymster FP, Hurley DJ, Potter WZ, Paul SM. Effects of xanomeline, a selective muscarinic receptor agonist,
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treatment approach for schizophrenia. <span><span class="ref-journal">Am. J. Psychiatry. </span>2008;<span class="ref-vol">165</span>:10331039.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/18593778" ref="pagearea=cite-ref&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubmed">PubMed<span class="bk_prnt">: 18593778</span></a>]</div></li><li><div class="bk_ref" id="ml071.r11">Spalding TA, Trotter C, Skajaerbaek N, Messier TL, Currier EA, Burstein ES, Li D, Hacksell U, Brann MR. Discovery of an ectopic site activation site on the M1 muscarinic
receptor. <span><span class="ref-journal">Mol. Pharm. </span>2002;<span class="ref-vol">61</span>:12971302.</span> [<a href="https://pubmed.ncbi.nlm.nih.gov/12021390" ref="pagearea=cite-ref&amp;targetsite=entrez&amp;targetcat=link&amp;targettype=pubmed">PubMed<span class="bk_prnt">: 12021390</span></a>]</div></li></ol></div><div id="bk_toc_contnr"></div></div></div>
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<div xmlns:np="http://ncbi.gov/portal/XSLT/namespace" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance"></div><div class="portlet"><div class="portlet_head"><div class="portlet_title"><h3><span>Views</span></h3></div><a name="Shutter" sid="1" href="#" class="portlet_shutter" title="Show/hide content" remembercollapsed="true" pgsec_name="PDF_download" id="Shutter"></a></div><div class="portlet_content"><ul xmlns:np="http://ncbi.gov/portal/XSLT/namespace" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" class="simple-list"><li><a href="/books/NBK47340/?report=reader">PubReader</a></li><li><a href="/books/NBK47340/?report=printable">Print View</a></li><li><a data-jig="ncbidialog" href="#_ncbi_dlg_citbx_NBK47340" data-jigconfig="width:400,modal:true">Cite this Page</a><div id="_ncbi_dlg_citbx_NBK47340" style="display:none" title="Cite this Page"><div class="bk_tt">Lindsley C, Lewis M, Weaver D. Discovery of a Highly Selective in vitro and in vivo M1 Allosteric Agonist Probe. 2008 Dec 3 [Updated 2010 Oct 4]. In: Probe Reports from the NIH Molecular Libraries Program [Internet]. Bethesda (MD): National Center for Biotechnology Information (US); 2010-. <span class="bk_cite_avail"></span></div></div></li><li><a href="/books/NBK47340/pdf/Bookshelf_NBK47340.pdf">PDF version of this page</a> (609K)</li></ul></div></div><div class="portlet"><div class="portlet_head"><div class="portlet_title"><h3><span>In this Page</span></h3></div><a name="Shutter" sid="1" href="#" class="portlet_shutter" title="Show/hide content" remembercollapsed="true" pgsec_name="page-toc" id="Shutter"></a></div><div class="portlet_content"><ul xmlns:np="http://ncbi.gov/portal/XSLT/namespace" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" class="simple-list"><li><a href="#ml071.s2" ref="log$=inpage&amp;link_id=inpage">Probe Structure &amp; Characteristics</a></li><li><a href="#ml071.s3" ref="log$=inpage&amp;link_id=inpage">Recommendations for the scientific use of this probe</a></li><li><a href="#ml071.s11" ref="log$=inpage&amp;link_id=inpage">PubChem Primary Assay 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