Investigations into the ability of the peptide, HAL18, to interact with bacterial membranes

被引:15
作者
Dennison, Sarah R. [1 ]
Kim, Young Soo [2 ]
Cha, Hyung Joon [2 ]
Phoenix, David A. [1 ]
机构
[1] Univ Cent Lancashire, Fac Sci & Technol, Preston PR1 2HE, Lancs, England
[2] Pohang Univ Sci & Technol, Dept Chem Engn, Pohang 790784, South Korea
来源
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 2008年 / 38卷 / 01期
关键词
Antimicrobial peptide; Monolayer stability; Peptide monolayer; Lipid-peptide interactions; Thermodynamic analysis;
D O I
10.1007/s00249-008-0352-6
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Halocidin was isolated from hemocytes, Halocynthia aurantium as a heterodimeric peptide consisting of two alpha-helical subunits, Hal15 and Hal18. Hal18 was shown to have antibacterial properties against Bacillus subtilis (MLC = 15 mu M) and Escherichia coli (MLC = 100 mu M). The peptide was shown to produce stable monolayers, which were characteristic of alpha-helical peptides predicted to orientate parallel to the surface of the interface. Constant area assays showed that Hal18 was surface active (4 mu M) inducing surface pressure changes > 30 mN m(-1) characteristic of membrane interactive peptides. The peptide induced stable surface pressure changes in monolayers that were mimetic of B. subtilis membranes (circa 7 mN m(-1)) and E. coli membrane-mimics (circa 4 mN m(-1)). Hal18 inserted readily into zwitterionic DOPE and anionic DOPG monolayers inducing surface pressure changes circa 8 mN m(-1) in both cases, providing evidence that interaction is not headgroup specific. Thermodynamic analysis of compression isotherms showed that the presence of Hal18 destabilised B. subtilis membranes (Delta G (Mix) > 0), which is in contrast to its stabilising effect on E. coli lipid extract implying the differential antimicrobial efficacy may be driven by lipid packing.
引用
收藏
页码:37 / 43
页数:7
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