Dennison, Sarah Rachel, Morton, Leslie Hugh Glyn, Shorrocks, Andrea Julie, Harris, Frederick and Phoenix, David Andrew
A study on the interactions of Aurein 2.5 with bacterial membranes.
Colloids and Surfaces B Biointerfaces, 68
Aurein 2.5 (GLFDIVKKVVGAFGSL-NH2) is an uncharacterised antimicrobial peptide. At an air/water interface, it exhibited strong surface activity (maximal surface pressure 25 mN m−1) and molecular areas consistent with the adoption of α-helical structure orientated either perpendicular (1.72 nm2 molecule−1) or parallel (3.6 nm2 molecule−1) to the interface. Aurein 2.5 was strongly antibacterial, exhibiting a minimum inhibitory concentration (MIC) of 30 μM against Bacillus subtilis and Escherichia coli. The peptide induced maximal surface pressure changes of 9 mN m−1 and 5 mN m−1, respectively, in monolayers mimicking membranes of these organisms whilst compression isotherm analysis of these monolayers showed ΔGMix > 0, indicating destabilisation by Aurein 2.5. These combined data suggested that toxicity of the peptide to these organisms may involve membrane invasion via the use of oblique orientated α-helical structure. The peptide induced strong, comparable maximal surface changes in monolayers of DOPG (7.5 mN m−1) and DOPE monolayers (6 mN m−1) suggesting that the membrane interactions of Aurein 2.5 were driven by amphiphilicity rather than electrostatic interaction. Based on these data, it was suggested that the differing ability of Aurein 2.5 to insert into membranes of B. subtilis and E. coli was probably related to membrane-based factors such as differences in lipid packing characteristics. The peptide was active against both sessile E. coli and Staphylococcus aureus with an MIC of 125 μM. The broad-spectrum antibacterial activity and non-specific modes of membrane action used by Aurein 2.5 suggested use as an anti-biofilm agent such as in the decontamination of medical devices.