De Novo designed 13 mer hairpin-peptide arrests insulin and inhibits its aggregation: role of OH–π interactions between water and hydrophobic amino acids-Reference-Cited by-同舟云学术

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De Novo designed 13 mer hairpin-peptide arrests insulin and inhibits its aggregation: role of OH–π interactions between water and hydrophobic amino acids

Published:2020 Issue:25 Volume:10 Page:14991-14999
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Mukherjee Meghomukta¹²³⁴,Banerjee Nilanjan¹²³⁴,Chatterjee Subhrangsu¹²³⁴^ORCID

Affiliation:

1. Department of Biophysics

2. Bose Institute

3. Kolkata 700054

4. India

Abstract

Protein aggregation in the cellular systems can be highly fatal causing a series of diseases including neurodegenerative diseases like ALS, Alzheimer, Prion Diseases, Parkinson's and other diseases like type II diabetes.

Funder

Department of Science and Technology, Ministry of Science and Technology, India

Council of Scientific and Industrial Research, India

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/RA/D0RA00832J

Reference34 articles.

1. Protein folding and misfolding

2. Review: History of the Amyloid Fibril

3. Oligomeric Forms of Insulin Amyloid Aggregation Disrupt Outgrowth and Complexity of Neuron-Like PC12 Cells

4. Designing conditions for in vitro formation of amyloid protofilaments and fibrils

5. A Three-Stage Kinetic Model of Amyloid Fibrillation

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