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Antimicrobial peptide (Cn‐AMP2) from liquid endosperm of Cocos nucifera forms amyloid‐like fibrillar structure
Author(s) -
Gour Shalini,
Kaushik Vibha,
Kumar Vijay,
Bhat Priyanka,
Yadav Subhash C.,
Yadav Jay K.
Publication year - 2016
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2860
Subject(s) - thioflavin , peptide , chemistry , cocos nucifera , endosperm , amyloid (mycology) , in silico , congo red , fibril , antimicrobial , biophysics , circular dichroism , biochemistry , organic chemistry , biology , medicine , inorganic chemistry , botany , disease , pathology , adsorption , gene , alzheimer's disease
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.