Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives

Fibrillar aggregates of human islet amyloid polypeptide, hIAPP, a pathological feature seen in some diabetes patients, are a likely causative agent for pancreatic beta-cell toxicity, leading to a transition from a state of insulin resistance to type II diabetes through the loss of insulin producing...

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Main Authors:	Pithadia, Amit, Brender, Jeffrey R., Fierke, Carol A., Ramamoorthy, Ayyalusamy
Format:	Online
Language:	English
Published:	Hindawi Publishing Corporation 2016
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4662995/

id	pubmed-4662995
recordtype	oai_dc
spelling	pubmed-46629952015-12-08 Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives Pithadia, Amit Brender, Jeffrey R. Fierke, Carol A. Ramamoorthy, Ayyalusamy Review Article Fibrillar aggregates of human islet amyloid polypeptide, hIAPP, a pathological feature seen in some diabetes patients, are a likely causative agent for pancreatic beta-cell toxicity, leading to a transition from a state of insulin resistance to type II diabetes through the loss of insulin producing beta-cells by hIAPP induced toxicity. Because of the probable link between hIAPP and the development of type II diabetes, there has been strong interest in developing reagents to study the aggregation of hIAPP and possible therapeutics to block its toxic effects. Natural products are a class of compounds with interesting pharmacological properties against amyloids which have made them interesting targets to study hIAPP. Specifically, the ability of polyphenolic natural products, EGCG, curcumin, and resveratrol, to modulate the aggregation of hIAPP is discussed. Furthermore, we have outlined possible mechanistic discoveries of the interaction of these small molecules with the peptide and how they may mitigate toxicity associated with peptide aggregation. These abundantly found agents have been long used to combat diseases for many years and may serve as useful templates toward developing therapeutics against hIAPP aggregation and toxicity. Hindawi Publishing Corporation 2016 2015-11-15 /pmc/articles/PMC4662995/ /pubmed/26649317 http://dx.doi.org/10.1155/2016/2046327 Text en Copyright © 2016 Amit Pithadia et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Pithadia, Amit Brender, Jeffrey R. Fierke, Carol A. Ramamoorthy, Ayyalusamy
spellingShingle	Pithadia, Amit Brender, Jeffrey R. Fierke, Carol A. Ramamoorthy, Ayyalusamy Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives
author_facet	Pithadia, Amit Brender, Jeffrey R. Fierke, Carol A. Ramamoorthy, Ayyalusamy
author_sort	Pithadia, Amit
title	Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives
title_short	Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives
title_full	Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives
title_fullStr	Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives
title_full_unstemmed	Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives
title_sort	inhibition of iapp aggregation and toxicity by natural products and derivatives
description	Fibrillar aggregates of human islet amyloid polypeptide, hIAPP, a pathological feature seen in some diabetes patients, are a likely causative agent for pancreatic beta-cell toxicity, leading to a transition from a state of insulin resistance to type II diabetes through the loss of insulin producing beta-cells by hIAPP induced toxicity. Because of the probable link between hIAPP and the development of type II diabetes, there has been strong interest in developing reagents to study the aggregation of hIAPP and possible therapeutics to block its toxic effects. Natural products are a class of compounds with interesting pharmacological properties against amyloids which have made them interesting targets to study hIAPP. Specifically, the ability of polyphenolic natural products, EGCG, curcumin, and resveratrol, to modulate the aggregation of hIAPP is discussed. Furthermore, we have outlined possible mechanistic discoveries of the interaction of these small molecules with the peptide and how they may mitigate toxicity associated with peptide aggregation. These abundantly found agents have been long used to combat diseases for many years and may serve as useful templates toward developing therapeutics against hIAPP aggregation and toxicity.
publisher	Hindawi Publishing Corporation
publishDate	2016
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4662995/
_version_	1613507338086383616

Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives

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