Tea catechins induce the conversion of preformed lysozyme amyloid fibrils to amorphous aggregates
- PMID: 19904937
- DOI: 10.1021/jf902664f
Tea catechins induce the conversion of preformed lysozyme amyloid fibrils to amorphous aggregates
Abstract
Natural polyphenols are major constituents of plant foods and herbs. Numerous studies have demonstrated that natural polyphenols inhibited amyloid formation and destabilized the preformed amyloid fibrils. However, the molecular mechanism for the antiamyloidogenesis of polyphenols is still unclear and remains to be further explored. In the present study, the preformed lysozyme fibrils were used as an in vitro model to study the disruptive effects of tea catechins on amyloid fibrils. Results showed that tea catechins induced the conversion of lysozyme fibrils to amorphous aggregates and inhibited fibril-induced hemolysis. Hydroquinone also showed disruptive effect on the fibrils, whereas phenol and two typical antioxidants, ascorbic acid and alpha-tocopherol, did not affect the fibrillar structure, suggesting that polyphenolic structure is essential for fibril deposition. Correlation analyses indicate that the fibril-depositing effects were related to both the antioxidative potency and hydrophobicity of tea catechins. These findings provide new evidence for comprehensive understanding of the interaction between natural polyphenols and amyloid fibrils.
Similar articles
-
Quinopeptide formation associated with the disruptive effect of epigallocatechin-gallate on lysozyme fibrils.Int J Biol Macromol. 2015;78:389-95. doi: 10.1016/j.ijbiomac.2015.04.031. Epub 2015 Apr 27. Int J Biol Macromol. 2015. PMID: 25931397
-
Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme.Biomacromolecules. 2004 Jul-Aug;5(4):1362-70. doi: 10.1021/bm0498979. Biomacromolecules. 2004. PMID: 15244452
-
Identification of the core structure of lysozyme amyloid fibrils by proteolysis.J Mol Biol. 2006 Aug 18;361(3):551-61. doi: 10.1016/j.jmb.2006.06.055. Epub 2006 Jul 7. J Mol Biol. 2006. PMID: 16859705
-
Protein amyloidose misfolding: mechanisms, detection, and pathological implications.Methods Mol Biol. 2005;300:417-35. doi: 10.1385/1-59259-858-7:417. Methods Mol Biol. 2005. PMID: 15657495 Review.
-
The chemistry of low molecular weight black tea polyphenols.Nat Prod Rep. 2010 Mar;27(3):417-62. doi: 10.1039/b912523j. Epub 2010 Feb 10. Nat Prod Rep. 2010. PMID: 20179879 Review.
Cited by
-
Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286).J Phys Chem B. 2012 Mar 22;116(11):3650-8. doi: 10.1021/jp2121577. Epub 2012 Mar 7. J Phys Chem B. 2012. PMID: 22360607 Free PMC article.
-
Development and In Vitro Evaluation of Linear PEI-Shelled Heparin/Berberine Nanoparticles in Human Osteosarcoma U-2 OS Cells.Molecules. 2018 Nov 28;23(12):3122. doi: 10.3390/molecules23123122. Molecules. 2018. PMID: 30487471 Free PMC article.
-
Efficient inhibition of amyloid fibrillation and cytotoxicity of α-synuclein and human insulin using biosynthesized silver nanoparticles decorated by green tea polyphenols.Sci Rep. 2024 Feb 16;14(1):3907. doi: 10.1038/s41598-024-54464-4. Sci Rep. 2024. PMID: 38365968 Free PMC article.
-
Trehalose and Magnesium Chloride Exert a Common Anti-amyloidogenic Effect Towards Hen Egg White Lysozyme.Protein J. 2017 Apr;36(2):138-146. doi: 10.1007/s10930-017-9705-2. Protein J. 2017. PMID: 28299593
-
Alternative pathways of human islet amyloid polypeptide aggregation distinguished by (19)f nuclear magnetic resonance-detected kinetics of monomer consumption.Biochemistry. 2012 Oct 16;51(41):8154-62. doi: 10.1021/bi3012548. Epub 2012 Oct 1. Biochemistry. 2012. PMID: 22998665 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
