title: The effect of amidation on the behaviour of antimicrobial peptides.
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 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.
authors.affiliation: Computational Physics Group, School of Mathematics and Physics, University of Lincoln, Brayford Pool, Lincoln, LN6 7TS, UK. mmura@lincoln.ac.uk.
authors.forename: Manuela
authors.identifier: http://orcid.org/0000-0002-3913-7595
authors.initials: M
authors.lastname: Mura
authors.affiliation: UCLan Biomedical Technology Limited (Shenzhen), Shenzhen Virtual University Park, Shenzhen, 518057, People's Republic of China.
authors.forename: Jianping
authors.initials: J
authors.lastname: Wang
authors.affiliation: UCLan Biomedical Technology Limited (Shenzhen), Shenzhen Virtual University Park, Shenzhen, 518057, People's Republic of China.
authors.forename: Yuhua
authors.initials: Y
authors.lastname: Zhou
authors.affiliation: Computational Physics Group, School of Mathematics and Physics, University of Lincoln, Brayford Pool, Lincoln, LN6 7TS, UK.
authors.forename: Marco
authors.initials: M
authors.lastname: Pinna
authors.affiliation: Computational Physics Group, School of Mathematics and Physics, University of Lincoln, Brayford Pool, Lincoln, LN6 7TS, UK.
authors.forename: Andrei V
authors.initials: AV
authors.lastname: Zvelindovsky
authors.affiliation: School of Pharmacy and Biomedical Science, University of Central Lancashire, Preston, PR1 2HE, UK.|School of Applied Science, London South Bank University, 103 Borough Road, London, SE1 0AA, UK.
authors.forename: Sarah R
authors.initials: SR
authors.lastname: Dennison
authors.affiliation: School of Applied Science, London South Bank University, 103 Borough Road, London, SE1 0AA, UK.
authors.forename: David A
authors.initials: DA
authors.lastname: Phoenix
mesh_terms: D000577:Amides / Q000737:chemistry; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry; D056004:Molecular Dynamics Simulation
chemical_list: D000577:Amides; D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D004134:Dimyristoylphosphatidylcholine
keywords: Amino acid; Anticancer; Antimicrobial peptides; Cooperative effect; Membrane; Molecular dynamics; Secondary structure