The effect of amidation on the behaviour of antimicrobial peptides

Mura, Manuela, Wang, Jianping, Zhou, Yuhua , Pinna, Marco, Zvelindovsky, Andrei V., Dennison, Sarah R. and Phoenix, David A. (2016) The effect of amidation on the behaviour of antimicrobial peptides. European Biophysics Journal, 45 (3). pp. 195-207. ISSN 0175-7571

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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 α-helical structure in solution (<30 %) and in the
presence of a lipid bilayer the peptides formed a stable α
-helical structure. In general, amidated analogues have a
greater propensity than the non-amidated peptides to form
a α-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-
CONH2 and aurein 3.1-CONH2 formed a helix horizontal
to the plane of an asymmetric interface.

Keywords:Antimicrobial peptides, Membrane, Molecular dynamics, Secondary structure, Cooperative effect, Amino acid, Anticancer, JCOpen
Subjects:C Biological Sciences > C700 Molecular Biology, Biophysics and Biochemistry
Divisions:College of Science > School of Mathematics and Physics
ID Code:20092
Deposited On:28 Jan 2016 17:25

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