Inhibition of Alzheimer's amyloid-β peptide aggregation and its disruption by a conformationally restricted α/β hybrid peptide. Issue 12 (17th December 2014)

• Record Type: Journal Article
• Authors: Paul, Ashim; Nadimpally, Krishna Chaitanya; Mondal, Tanmay; Thalluri, Kishore; Mandal, Bhubaneswar
• Is Part Of: Chemical communications. Volume 51:Issue 12(2015)
• Page Start: 2245
• Page End: 2248
• Publication Date: 2014-12-17
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c4cc09063b
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : A novel class of anthranilic acid containing a conformationally restricted β-sheet breaker α/β-hybrid peptide efficiently disrupts preformed fibrillar aggregates of Aβ1–40 in vitro . Abstract : Insertion of an anthranilic acid in an amyloidogenic peptide sequence generates a novel conformationally restricted α/β-hybrid peptide that inhibits amyloid formation of Aβ(1–40) and disrupts preformed fibrillar aggregates in vitro . Such β-sheet breaker hybrid peptides (BSBHps) may be useful for designing novel physiologically important compounds relevant to diverse amyloidoses and for studying the process of aggregation.