The effect of amidation on the behaviour of antimicrobial peptides

Journal article

Mura, M, Wang, J, Zhou, Y, Pinna, M, Zvelindovsky, A, Dennison, SR and Phoenix, DA (2016). The effect of amidation on the behaviour of antimicrobial peptides. European Biophysics Journal. 45 (3), pp. 195-207. https://doi.org/10.1007/s00249-015-1094-x
AuthorsMura, M, Wang, J, Zhou, Y, Pinna, M, Zvelindovsky, A, Dennison, SR and Phoenix, DA
Abstract

Aurein 2.6-COOH and aurein 3.1-COOH were studied along with their naturally occurring C-terminally amidated analogues. Circular dichroism (CD) and molecular dynamic (MD) simulations were used to study the effects of amidation on the interaction of antimicrobial peptides (AMPs) with lipid bilayers. CD measurements and MD analysis suggested that both peptide analogues were predominantly random coil and adopted low levels of (Formula presented.)-helical structure in solution (<30 %) and in the presence of a lipid bilayer the peptides formed a stable (Formula presented.)-helical structure. In general, amidated analogues have a greater propensity than the non-amidated peptides to form a (Formula presented.)-helical structure. MD simulations predicted that aurein 2.6-COOH and aurein 3.1-CHOOH destabilised lipid bilayers from 1,2-dimyristoyl-sn-glycero-3-phosphocholine and 1,2-dimyristoyl-sn-glycero-3-phosphoserine via angled bilayer penetration. They also showed that aurein 2.6-CONH(Formula presented.) and aurein 3.1-CONH(Formula presented.) formed a helix horizontal to the plane of an asymmetric interface. © 2016 The Author(s)

KeywordsAmino acids; Amino acid; Anticancer; Antimicrobial peptides; Cooperative effect; Membrane; Molecular dynamics; Secondary structure
Year2016
JournalEuropean Biophysics Journal
Journal citation45 (3), pp. 195-207
PublisherSpringer
ISSN0175-7571
Digital Object Identifier (DOI)https://doi.org/10.1007/s00249-015-1094-x
Funder/ClientVolkswagen Foundation
Publication dates
Print08 Jan 2016
Publication process dates
Deposited14 Apr 2016
Accepted20 Oct 2015
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