Pristine and Hydroxylated Fullerenes Prevent the Aggregation of Human Islet Amyloid Polypeptide and Display Different Inhibitory Mechanisms-Reference-Cited by-同舟云学术

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Pristine and Hydroxylated Fullerenes Prevent the Aggregation of Human Islet Amyloid Polypeptide and Display Different Inhibitory Mechanisms

Published:2020-02-05 Issue: Volume:8 Page:
ISSN:2296-2646
Container-title:Frontiers in Chemistry
language:
Short-container-title:Front. Chem.

Author:

Bai Cuiqin,Lao Zenghui,Chen Yujie,Tang Yiming,Wei Guanghong

Funder

National Science Foundation

National Key Research and Development Program of China Stem Cell and Translational Research

Publisher

Frontiers Media SA

Subject

General Chemistry

Reference69 articles.

1. A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor;Abedini;J. Am. Chem. Soc.,2007

2. Amyloid-beta fibril disruption by C60-molecular guidance for rational drug design;Andujar;Phys. Chem. Chem. Phys.,2012

3. Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. an experimental support for the key role of the phenylalanine residue in amyloid formation;Azriel;J. Biol. Chem.,2001

4. Influence of fullerenol on hIAPP aggregation: amyloid inhibition and mechanistic aspects;Bai;Phys. Chem. Chem. Phys.,2019

5. Fullerenol C-60(OH)(16) prevents amyloid fibrillization of a beta(40)–in vitro and in silico approach;Bednarikova;Phys. Chem. Chem. Phys.,2016

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