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Literature DB >> 19165839

Inhibiting islet amyloid polypeptide fibril formation by the red wine compound resveratrol.

Rajesh Mishra¹, Daniel Sellin, Diana Radovan, Andrea Gohlke, Roland Winter.

Abstract

GRAPES FOR AMYLOIDS: The red wine compound resveratrol can effectively inhibit the formation of IAPP amyloid that is found in type II diabetes. Our in vitro inhibition results do not depend on the antioxidant activity of resveratrol. Further, the markedly enhanced cell survival in the presence of resveratrol also indicates that the small oligomeric structures that are observed during beta-sheet formation are not toxic and could be off-pathway assembly products.

Entities: Chemical Disease Gene

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Year: 2009 PMID： 19165839 DOI： 10.1002/cbic.200800762

Source DB: PubMed Journal: Chembiochem ISSN： 1439-4227 Impact factor: 3.164

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Cited

45 in total

1. Single-molecule fluorescence spectroscopy using phospholipid bilayer nanodiscs.

Authors: Abhinav Nath; Adam J Trexler; Peter Koo; Andrew D Miranker; William M Atkins; Elizabeth Rhoades
Journal: Methods Enzymol Date: 2010 Impact factor: 1.600

2. Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediates.

Authors: Fanling Meng; Daniel P Raleigh
Journal: J Mol Biol Date: 2010-12-30 Impact factor: 5.469

Inhibiting islet amyloid polypeptide fibril formation by the red wine compound resveratrol.

1. Single-molecule fluorescence spectroscopy using phospholipid bilayer nanodiscs.

2. Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediates.

3. Graphene oxide inhibits hIAPP amyloid fibrillation and toxicity in insulin-producing NIT-1 cells.

4. Probing the binding affinity of amyloids to reduce toxicity of oligomers in diabetes.

Review 5. Implications of peptide assemblies in amyloid diseases.

Review 6. Inhibition of protein misfolding and aggregation by natural phenolic compounds.

Review 7. Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.

8. Blockade of islet amyloid polypeptide fibrillation and cytotoxicity by the secretory chaperones 7B2 and proSAAS.

9. Folded small molecule manipulation of islet amyloid polypeptide.

10. Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status.