Literature DB >> 18529009

Water-soluble tripeptide Abeta (9-11) forms amyloid-like fibrils and exhibits neurotoxicity.

Jishu Naskar1, Michael G B Drew, Ishani Deb, Sumantra Das, Arindam Banerjee.   

Abstract

A water-soluble, hydrophilic tripeptide GYE, having sequence identity with the N-terminal segment of amyloid peptides Abeta(9-11), upon self-association exhibits amyloid-like fibrils and significant neurotoxicity towards the Neuro2A cell line. However, the tripeptides GFE and GWE, in which the centrally located tyrosine residue has been replaced by phenylalanine or tryptophan, fail to show amyloidogenic behavior and exhibit little or no neurotoxicity.

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Year:  2008        PMID: 18529009     DOI: 10.1021/ol8007217

Source DB:  PubMed          Journal:  Org Lett        ISSN: 1523-7052            Impact factor:   6.005


  2 in total

1.  Probing the role of aromatic residues in the self-assembly of Aβ(16-22) in fluorinated alcohols and their aqueous mixtures.

Authors:  Sanjai Kumar Pachahara; Ramakrishnan Nagaraj
Journal:  Biochem Biophys Rep       Date:  2015-04-25

2.  Distinct position-specific sequence features of hexa-peptides that form amyloid-fibrils: application to discriminate between amyloid fibril and amorphous β-aggregate forming peptide sequences.

Authors:  A Mary Thangakani; Sandeep Kumar; D Velmurugan; M Michael Gromiha
Journal:  BMC Bioinformatics       Date:  2013-05-09       Impact factor: 3.169

  2 in total

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