Interaction of antimicrobial peptides with lipopolysaccharides

被引:102
作者
Ding, L
Yang, L
Weiss, TM
Waring, AJ
Lehrer, RI
Huang, HW [1 ]
机构
[1] Rice Univ, Dept Phys & Astron, Houston, TX 77251 USA
[2] Univ Calif Los Angeles, Dept Med, Sch Med, Los Angeles, CA 90095 USA
[3] Univ Calif Los Angeles, Dept Pediat, Sch Med, Los Angeles, CA 90095 USA
关键词
D O I
10.1021/bi035130+
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We study the interaction of antimicrobial peptides with lipopolysaccharide (LPS) bilayers to understand how antimicrobial peptides interact with the LPS monolayer on the outer membrane of Gram-negative bacteria. LPS in water spontaneously forms a multilamellar structure composed of symmetric bilayers. We performed X-ray lamellar diffraction and wide-angle in-plane scattering to study the physical characteristics of LPS multilayers. The multilayer alignment of LPS is comparable to phospholipids. Thus, it is suitable for the application of oriented circular dichroism (OCD) to study the state of peptides in LPS bilayers. At high hydration levels, the chain melting temperature in multilamella detected by X-ray diffraction is the same as that of LPS aqueous dispersions, as measured by calorimetry. LPS has a strong CD, but with a careful subtraction of the lipid background, the OCD of peptides in LPS is measurable. The method was tested successfully with melittin. It was then applied to two representative antimicrobial peptides, magainin and protegrin. At peptide concentrations comparable to the physiological conditions, both peptides penetrate transmembrane in LPS bilayers. The results imply that antimicrobial peptides readily penetrate the LPS monolayer of the outer membrane.
引用
收藏
页码:12251 / 12259
页数:9
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