Potential of peptides and phytochemicals in attenuating different phases of islet amyloid polypeptide fibrillation for type 2 diabetes management
Islet amyloid polypeptide (IAPP), or amylin, has been identified as a key factor in the development of type 2 diabetes (T2D). IAPP aggregates, which form amyloid fibrils, contribute to cytotoxicity of the pancreatic β-cells, resulting in loss of function and subsequent reduction in insulin productio...
Saved in:
Main Authors: | , |
---|---|
Format: | Article |
Language: | English |
Published: |
Tsinghua University Press
2021-05-01
|
Series: | Food Science and Human Wellness |
Subjects: | |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2213453021000264 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
_version_ | 1832557599123308544 |
---|---|
author | Raliat O. Abioye Chibuike C. Udenigwe |
author_facet | Raliat O. Abioye Chibuike C. Udenigwe |
author_sort | Raliat O. Abioye |
collection | DOAJ |
description | Islet amyloid polypeptide (IAPP), or amylin, has been identified as a key factor in the development of type 2 diabetes (T2D). IAPP aggregates, which form amyloid fibrils, contribute to cytotoxicity of the pancreatic β-cells, resulting in loss of function and subsequent reduction in insulin production. As a result, surviving β-cells overcompensate for this reduction of insulin production, further contributing to the loss of function because of increased stress, thus leading to insulin resistance. Endogenously, IAPP monomers function in a variety of roles; however, aggregation renders them non-functional. The use of naturally occurring compounds, including peptides and phytochemicals, has been explored as a way to mitigate or inhibit IAPP fibril formation. This review discusses the structure, endogenous roles and mechanism of IAPP fibril formation, recent advances on inhibitors of IAPP fibril formation, and new insights on the future development and application of food-derived inhibitors towards T2D management. |
format | Article |
id | doaj-art-bdd09441a2054fab96a1680c46c049a4 |
institution | Kabale University |
issn | 2213-4530 |
language | English |
publishDate | 2021-05-01 |
publisher | Tsinghua University Press |
record_format | Article |
series | Food Science and Human Wellness |
spelling | doaj-art-bdd09441a2054fab96a1680c46c049a42025-02-03T04:08:07ZengTsinghua University PressFood Science and Human Wellness2213-45302021-05-01103259269Potential of peptides and phytochemicals in attenuating different phases of islet amyloid polypeptide fibrillation for type 2 diabetes managementRaliat O. Abioye0Chibuike C. Udenigwe1Department of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, Ontario, K1N 6N5, CanadaDepartment of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, Ontario, K1N 6N5, Canada; School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, Ottawa, Ontario, K1H 8M5, Canada; Corresponding author. University Research Chair in Food Properties and Nutrient Bioavailability, School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, Ottawa, Ontario, K1H 8M5, Canada.Islet amyloid polypeptide (IAPP), or amylin, has been identified as a key factor in the development of type 2 diabetes (T2D). IAPP aggregates, which form amyloid fibrils, contribute to cytotoxicity of the pancreatic β-cells, resulting in loss of function and subsequent reduction in insulin production. As a result, surviving β-cells overcompensate for this reduction of insulin production, further contributing to the loss of function because of increased stress, thus leading to insulin resistance. Endogenously, IAPP monomers function in a variety of roles; however, aggregation renders them non-functional. The use of naturally occurring compounds, including peptides and phytochemicals, has been explored as a way to mitigate or inhibit IAPP fibril formation. This review discusses the structure, endogenous roles and mechanism of IAPP fibril formation, recent advances on inhibitors of IAPP fibril formation, and new insights on the future development and application of food-derived inhibitors towards T2D management.http://www.sciencedirect.com/science/article/pii/S2213453021000264Islet amyloid polypeptideFibril formationDisaggregationBioactive peptidesPhytochemicals |
spellingShingle | Raliat O. Abioye Chibuike C. Udenigwe Potential of peptides and phytochemicals in attenuating different phases of islet amyloid polypeptide fibrillation for type 2 diabetes management Food Science and Human Wellness Islet amyloid polypeptide Fibril formation Disaggregation Bioactive peptides Phytochemicals |
title | Potential of peptides and phytochemicals in attenuating different phases of islet amyloid polypeptide fibrillation for type 2 diabetes management |
title_full | Potential of peptides and phytochemicals in attenuating different phases of islet amyloid polypeptide fibrillation for type 2 diabetes management |
title_fullStr | Potential of peptides and phytochemicals in attenuating different phases of islet amyloid polypeptide fibrillation for type 2 diabetes management |
title_full_unstemmed | Potential of peptides and phytochemicals in attenuating different phases of islet amyloid polypeptide fibrillation for type 2 diabetes management |
title_short | Potential of peptides and phytochemicals in attenuating different phases of islet amyloid polypeptide fibrillation for type 2 diabetes management |
title_sort | potential of peptides and phytochemicals in attenuating different phases of islet amyloid polypeptide fibrillation for type 2 diabetes management |
topic | Islet amyloid polypeptide Fibril formation Disaggregation Bioactive peptides Phytochemicals |
url | http://www.sciencedirect.com/science/article/pii/S2213453021000264 |
work_keys_str_mv | AT raliatoabioye potentialofpeptidesandphytochemicalsinattenuatingdifferentphasesofisletamyloidpolypeptidefibrillationfortype2diabetesmanagement AT chibuikecudenigwe potentialofpeptidesandphytochemicalsinattenuatingdifferentphasesofisletamyloidpolypeptidefibrillationfortype2diabetesmanagement |