B
Bibin G. Anand
Researcher at Jawaharlal Nehru University
Publications - 38
Citations - 656
Bibin G. Anand is an academic researcher from Jawaharlal Nehru University. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 11, co-authored 29 publications receiving 416 citations. Previous affiliations of Bibin G. Anand include University of Alberta & Indian Institute of Technology, Jodhpur.
Papers
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Journal ArticleDOI
Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin.
Kriti Dubey,Bibin G. Anand,Rahul Badhwar,Ganesh Bagler,P. N. Navya,Hemant Kumar Daima,Karunakar Kar +6 more
TL;DR: Stable gold and silver nanoparticles which are surface functionalized with either tyrosine or tryptophan residues and have examined their potential to inhibit amyloid aggregation of insulin offer significant opportunities for developing nanoparticle-based therapeutics against diseases related to protein aggregation.
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Biosynthesis of silver nano-particles by marine sediment fungi for a dose dependent cytotoxicity against HEp2 cell lines
TL;DR: The strains, SP3, SP4, SP5, and SP6 could be used for simple, non-hazardous and efficient synthesis of antimicrobial and HEp2 cytotoxic silver nano-particles.
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Eugenol prevents amyloid formation of proteins and inhibits amyloid-induced hemolysis.
TL;DR: The inherent ability of eugenol to stabilize native proteins and to delay the conversion of protein species of native conformation into β-sheet assembled mature fibrils seems to be crucial for its inhibitory effect.
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Capsaicin-Coated Silver Nanoparticles Inhibit Amyloid Fibril Formation of Serum Albumin
TL;DR: It is found that amyloid formation of BSA was strongly suppressed in the presence of AgNPs(Cap), but isolated capsaicin and uncapped control nanoparticles did not show such an inhibition effect, suggesting the significance of surface functionalization of nanoparticles with Capsaicin.
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Intrinsic property of phenylalanine to trigger protein aggregation and hemolysis has a direct relevance to phenylketonuria
TL;DR: Cross-seeding ability of phenylalanine fibrils are shown that can effectively initiate an aggregation process in proteins under physiological conditions, converting native protein structures to β-sheet assembly.