Quantification of protein aggregation rates and quenching effects of amylin–inhibitor complexes
Author:
Affiliation:
1. Department of Physics
2. Indian Institute of Technology Kharagpur
3. Kharagpur-721302
4. India
5. School of Nanoscience and Technology
Abstract
Comparative inhibition capabilities of graphene quantum dots, resveratrol, and curcumin decipher the dose-dependent competitive role of protein aggregation rate and quenching effect in amylin fibrillation.
Funder
Max-Planck-Gesellschaft
Science and Engineering Research Board
Indian Institute of Technology Kharagpur
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2019/CP/C9CP03238J
Reference73 articles.
1. D. Whitford , Proteins: structure and function , John Wiley & Sons , 2013
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4. Type 2 diabetes as a protein misfolding disease
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