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<title>a Microarray-based approach for the development of RNA-binding small molecules with anti-HIV activity | NIH Research Festival</title>
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<article><div class="banner banner--gray banner--compact" style="--banner-background-image: url('/sites/default/files/media/image/2021-03/2015.jpg');--banner-background-focus: 50% 50%"><div class="banner__wrapper"><div class="banner__container"><h2 class="banner__heading">NIH Research Festival</h2><div class="banner__content"><p><strong><time datetime="2015-09-16">September 16</time> – <time datetime="2015-09-18">18, 2015</time></strong></p></div></div></div></div></article>
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<div class="section"><div data-drupal-messages-fallback class="hidden"></div></div><main role="main"><div id="main-content" tabindex="-1"></div><div class="section"><div class="content-sidebar"><div class="content-sidebar__main"><div class="content-sidebar__main-content"><div id="block-mainpagecontent-2"><article><h1>a Microarray-based approach for the development of RNA-binding small molecules with anti-HIV activity</h1><div class="schedule"><div class="schedule__label"><div class="schedule__label-text"><time datetime="2015-09-17">Thursday, September 17, 2015</time>
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– Poster Session II
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</div></div><div class="schedule__content"><div class="schedule__item"><div class="schedule__time">12:00 – 1:30 p.m.</div><div class="schedule__description"><p><strong>FAES Terrace</strong></p></div><div class="schedule__description"><p><strong>NCI</strong></p></div><div class="schedule__description"><p><strong>CHEMBIO-1</strong></p></div></div></div></div><p><strong>FARE Award Winner</strong></p><h2>Authors</h2><ul><li>FA Abulwerdi</li><li>R van Duyne</li><li>J Sztuba-Solinska</li><li>EO Freed</li><li>SFJ Le Grice</li><li>JS Schneekloth Jr</li></ul><h2>Abstract</h2><p>The HIV-1 trans-activation response (TAR) element RNA has long been considered a target for inhibiting virus replication, however most known TAR binders are highly charged compounds or aminoglycosides that lack selectivity. As part of an effort to find drug-like small molecules that bind TAR, we utilized a small molecule microarray screening approach. This work resulted in the identification of a novel thienopyridine scaffold that selectivity binds to TAR. Herein we report a 3-step synthetic route to generate a library of thirty analogs to improve potency and establish a structure-activity relationship. Analogs were evaluated in several complementary biochemical, biophysical and cell-based assays. Assessment of the analogs in a Thermofluor assay showed that the majority of analogs caused a 1-2o decrease in Tm of TAR indicating that binding of this class of compounds causes destabilization of TAR. In addition, evaluation of analogs in a fluorescence intensity assay as well as an AlphaScreen-based competitive assay between a Tat peptide and TAR provided binding affinity and potency for all analogs. Analogs with a 1,3,4-oxadiazole linker bind to TAR and disrupt Tat/TAR complex in mid and low micromolar range respectively. Furthermore, one of the most potent analogs, 116FA, was evaluated in a Tat-mediated HIV-1 LTR-driven luciferase reporter assay and preliminary results suggest inhibition of transcription upon treatment with 10 μM of 116FA. In summary, a novel class of small-molecule TAR binders has been development that binds and destabilizes TAR. The most potent analogs are also able to disrupt Tat/TAR interaction in vitro and in cells.</p><p><strong>Scientific Focus Area</strong>: Chemical Biology</p><p class="updated"><small>This page was last updated on Friday, March 26, 2021</small></p></article>
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