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Cited by 282

The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.

The Flavanol (−)-Epigallocatechin 3-Gallate Inhibits Amyloid Formation by Islet Amyloid Polypeptide, Disaggregates Amyloid Fibrils, and Protects Cultured Cells against IAPP-Induced Toxicity

Open access
Meng, Fanling, Abedini, Andisheh, Plesner, Annette, Verchere, C. Bruce, Raleigh, Daniel P.·2010·Biochemistry
DOI 10.1021/bi100939a
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Abstract

Islet amyloid polypeptide (IAPP, amylin) is the major protein component of the islet amyloid deposits associated with type 2 diabetes. The polypeptide lacks a well-defined structure in its monomeric state but readily assembles to form amyloid. Amyloid fibrils formed from IAPP, intermediates generated in the assembly of IAPP amyloid, or both are toxic to β-cells, suggesting that islet amyloid formation may contribute to the pathology of type 2 diabetes. There are relatively few reported inhibitors of amyloid formation by IAPP. Here we show that the tea-derived flavanol, (-)-epigallocatechin 3-gallate [(2R,3R)-5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-3,4-dihydro-2H-1-benzopyran-3-yl 3,4,5-trihydroxybenzoate] (EGCG), is an effective inhibitor of in vitro IAPP amyloid formation and disaggregates preformed amyloid fibrils derived from IAPP. The compound is thus one of a very small set of molecules which have been shown to disaggregate IAPP amyloid fibrils. Fluorescence-detected thioflavin-T binding assays and transmission electron microscopy confirm that the compound inhibits unseeded amyloid fibril formation as well as disaggregates IAPP amyloid. Seeding studies show that the complex formed by IAPP and EGCG does not seed amyloid formation by IAPP. In this regard, the behavior of IAPP is similar to the reported interactions of Aβ and α-synuclein with EGCG. Alamar blue assays and light microscopy indicate that the compound protects cultured rat INS-1 cells against IAPP-induced toxicity. Thus, EGCG offers an interesting lead structure for further development of inhibitors of IAPP amyloid formation and compounds that disaggregate IAPP amyloid.

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Metadata

Authors
Meng, F., Abedini, A., Plesner, A., Verchere, C. B., & Raleigh, D. P.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2010-08-30
Volume
49
Issue
37
Pages
8127-8133
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi100939a
OpenAlex
W1982653993
Cited by
282
References
59
FWCI
11.41
Type
journal article
Language
en
Open access
green

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