Aβ1–42 C-terminus fragment derived peptides prevent the self-assembly of the parent peptide. Issue 7 (16th January 2017)

• Record Type: Journal Article
• Authors: Bansal, Sunil; Maurya, Indresh Kumar; Shenmar, Kitika; Yadav, Nitin; Thota, Chaitanya Kumar; Kumar, Vinod; Tikoo, Kulbhushan; Chauhan, Virander Singh; Jain, Rahul
• Is Part Of: RSC advances. Volume 7:Issue 7(2017)
• Page Start: 4167
• Page End: 4173
• Publication Date: 2017-01-16
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c6ra26295c
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : A series of peptides derived from the C-terminus fragment (Aβ38–42 ) of Aβ showed significant to complete reduction in Aβ-induced toxicity. Abstract : In an attempt to design Aβ aggregation inhibitors to combat Alzheimer's disease, herein we report a full peptide scan performed on a pentapeptide fragment (Aβ38–42 ) derived from the C-terminus of Aβ1–42 peptide. More than thirty new peptides were synthesized and tested for their inhibition activity towards Aβ self-assembly. In the cell viability assay, when co-incubated with Aβ, three peptides were found to completely prevent the toxicity induced by Aβ aggregation. Most active pentapeptides were also studied by ThT fluorescence assay and the results were well correlated to the MTT study. The inhibition potential of a pentapeptide (15 ) was further confirmed by CD spectroscopy and transmission electron microscopy.