Antimicrobial peptide (Cn‐AMP2) from liquid endosperm of Cocos nucifera forms amyloid‐like fibrillar structure. (1st March 2016)

• Record Type: Journal Article
• Authors: Gour, Shalini; Kaushik, Vibha; Kumar, Vijay; Bhat, Priyanka; Yadav, Subhash C.; Yadav, Jay K.
• Is Part Of: Journal of peptide science. Volume 22:Number 4(2016:Apr.)
• Page Start: 201
• Page End: 207
• Publication Date: 2016-03-01
• Subjects: antimicrobial peptides (AMPs) -- cross β structure -- amyloids -- oligomers; Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.2860
• Languages: English
• ISSNs: 1075-2617

Abstract

Abstract : Cn‐AMP2 is an antimicrobial peptide derived from liquid endosperm of coconut ( Cocos nucifera ). It consists of 11 amino acid residues and predicted to have high propensity for β‐sheet formation that disposes this peptide to be amyloidogenic. In the present study, we have examined the amyloidogenic propensities of Cn‐AMP2 in silico and then tested the predictions under in vitro conditions. The in silico study revealed that the peptide possesses high amyloidogenic propensity comparable with Aβ. Upon solubilisation and agitation in aqueous buffer, Cn‐AMP2 forms visible aggregates that display bathochromic shift in the Congo red absorbance spectra, strong increase in thioflavin T fluorescence and fibrillar morphology under transmission electron microscopy. All these properties are typical of an amyloid fibril derived from various proteins/peptides including Aβ. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd. Abstract : Cn‐AMP2 is an antimicrobial peptide present in liquid endosperm of Cocos nucifera . In this study, we have found that the peptide has high propensity for aggregation ( in silico analysis) and it forms well‐structured amyloid like fibrils under in vitro conditions, detected by Congo red absorbance and Thioflavin T fluorescence assays. The fibrillar morphology visualized by transmission electron microscopy is typical of amyloid fibrils.