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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Format: | Article |
Language: | English |
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Wiley
2016-01-01
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Series: | Journal of Diabetes Research |
Online Access: | http://dx.doi.org/10.1155/2016/2046327 |
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author | Amit Pithadia Jeffrey R. Brender Carol A. Fierke Ayyalusamy Ramamoorthy |
author_facet | Amit Pithadia Jeffrey R. Brender Carol A. Fierke Ayyalusamy Ramamoorthy |
author_sort | Amit Pithadia |
collection | DOAJ |
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. |
format | Article |
id | doaj-art-3c9ee08b91e64ab19b5c1f62fe872ceb |
institution | Kabale University |
issn | 2314-6745 2314-6753 |
language | English |
publishDate | 2016-01-01 |
publisher | Wiley |
record_format | Article |
series | Journal of Diabetes Research |
spelling | doaj-art-3c9ee08b91e64ab19b5c1f62fe872ceb2025-02-03T01:01:49ZengWileyJournal of Diabetes Research2314-67452314-67532016-01-01201610.1155/2016/20463272046327Inhibition of IAPP Aggregation and Toxicity by Natural Products and DerivativesAmit Pithadia0Jeffrey R. Brender1Carol A. Fierke2Ayyalusamy Ramamoorthy3Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USABiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USABiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USABiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USAFibrillar 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.http://dx.doi.org/10.1155/2016/2046327 |
spellingShingle | Amit Pithadia Jeffrey R. Brender Carol A. Fierke Ayyalusamy Ramamoorthy Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives Journal of Diabetes Research |
title | 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_short | Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives |
title_sort | inhibition of iapp aggregation and toxicity by natural products and derivatives |
url | http://dx.doi.org/10.1155/2016/2046327 |
work_keys_str_mv | AT amitpithadia inhibitionofiappaggregationandtoxicitybynaturalproductsandderivatives AT jeffreyrbrender inhibitionofiappaggregationandtoxicitybynaturalproductsandderivatives AT carolafierke inhibitionofiappaggregationandtoxicitybynaturalproductsandderivatives AT ayyalusamyramamoorthy inhibitionofiappaggregationandtoxicitybynaturalproductsandderivatives |