Dennison Sarah R, Morton Leslie H G, Harris Frederick, Phoenix David A
Faculty of Science and Technology, University of Central Lancashire, Preston PR1 2HE, UK.
Biophys Chem. 2007 Sep;129(2-3):279-83. doi: 10.1016/j.bpc.2007.06.007. Epub 2007 Jun 22.
Theoretical analysis indicates that peptide VP1 forms a membrane interactive amphiphilic alpha-helix with antibacterial properties. Fourier transform infra-red based analyses showed VP1 to be alpha-helical (45%) in the presence of vesicle mimics of membranes from Staphylococcus aureus and to induce increases in the fluidity of these vesicles, as indicated by a rise in wavenumber of circa 0.5 to 1.0 cm(-1). The peptide induced surface pressure increases of 5 mN m(-1) in monolayer mimics of S. aureus membranes confirm the formation of a membrane interactive alpha-helix. These interactions appeared to involve significant hydrophobic and electrostatic contributions as VP1 induced comparable surface pressure changes in anionic (5.5 mN m(-1)) and zwitterionic (4 mN m(-1)) lipid monolayers. It is suggested that whilst efficacy requires further sequence specific information, the peptides generic structure provides the basis for its broad antimicrobial activity.
理论分析表明，肽VP1形成具有抗菌特性的膜相互作用两亲性α-螺旋。基于傅里叶变换红外光谱的分析表明，在金黄色葡萄球菌膜的囊泡模拟物存在下，VP1呈α-螺旋结构（45%），并导致这些囊泡的流动性增加，波数增加约0.5至1.0 cm(-1)表明了这一点。该肽在金黄色葡萄球菌膜的单层模拟物中诱导表面压力增加5 mN m(-1)，证实了膜相互作用α-螺旋的形成。这些相互作用似乎涉及显著的疏水和静电作用，因为VP1在阴离子（5.5 mN m(-1)）和两性离子（4 mN m(-1)）脂质单层中诱导了相当的表面压力变化。有人认为，虽然疗效需要进一步的序列特异性信息，但该肽的通用结构为其广泛的抗菌活性提供了基础。
