Abstract
Aurein 2.5 (GLFDIVKKVVGAFGSL-NH2) is an amphibian antimicrobial peptide. Here, characterisation studies showed the peptide to exhibit molecular areas at an air / water interface (1.77 - 3.1 nm2), which are in agreement with the adoption of α-helical structures. Lipid monolayer studies showed aurein 2.5 to induce maximal surface pressure changes of circa 7 mN m-1 in monolayers formed from phosphatidylglycerol (PG) and circa 6 mN m-1 in those formed from phosphatidylethanolamine (PE). These data indicate that the membrane interactions of the peptide are amphiphilicity driven with no apparent electrostatic requirement. Individually mutating the phenylalanine residues of aurein 2.5 to leucine had no major effect on the levels of PG and PE interactions, suggesting that these residues are not essential to the membrane interactions of the peptide, contrasting to other aureins where corresponding phenylalanine residues are required for efficient membrane interaction and antibacterial activity. This difference in the requirement is suggested to relate to the surface architecture as proposed by the concept of the molecular perturbation potential.
Keywords: Antimicrobial peptide, Hydrophobic groove, Peptide monolayer, Peptide-lipid interactions
Protein & Peptide Letters
Title: A Study on the Importance of Phenylalanine for Aurein Functionality
Volume: 16 Issue: 12
Author(s): Sarah R. Dennison, Frederick Harris and David A. Phoenix
Affiliation:
Keywords: Antimicrobial peptide, Hydrophobic groove, Peptide monolayer, Peptide-lipid interactions
Abstract: Aurein 2.5 (GLFDIVKKVVGAFGSL-NH2) is an amphibian antimicrobial peptide. Here, characterisation studies showed the peptide to exhibit molecular areas at an air / water interface (1.77 - 3.1 nm2), which are in agreement with the adoption of α-helical structures. Lipid monolayer studies showed aurein 2.5 to induce maximal surface pressure changes of circa 7 mN m-1 in monolayers formed from phosphatidylglycerol (PG) and circa 6 mN m-1 in those formed from phosphatidylethanolamine (PE). These data indicate that the membrane interactions of the peptide are amphiphilicity driven with no apparent electrostatic requirement. Individually mutating the phenylalanine residues of aurein 2.5 to leucine had no major effect on the levels of PG and PE interactions, suggesting that these residues are not essential to the membrane interactions of the peptide, contrasting to other aureins where corresponding phenylalanine residues are required for efficient membrane interaction and antibacterial activity. This difference in the requirement is suggested to relate to the surface architecture as proposed by the concept of the molecular perturbation potential.
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Cite this article as:
Dennison R. Sarah, Harris Frederick and Phoenix A. David, A Study on the Importance of Phenylalanine for Aurein Functionality, Protein & Peptide Letters 2009; 16 (12) . https://dx.doi.org/10.2174/092986609789839340
DOI https://dx.doi.org/10.2174/092986609789839340 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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