Gromova I A, Molotkovsky J G, Bergelson L D
M.M. Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR, Moscow.
Chem Phys Lipids. 1992 Jan-Feb;60(3):235-46. doi: 10.1016/0009-3084(92)90075-z.
The interaction of melittin with multicomponent lipid mixtures composed of phosphatidylcholine, sphingomyelin and phosphatidylserine or phosphatidylglycerol was investigated by measuring the intrinsic fluorescence of the peptide, steady state fluorescence anisotropy of, and Trp-fluorescence energy transfer to fluorescent analogs of the same phospholipids bearing the anthrylvinyl fluorophore in one of the aliphatic chains at various distances from the polar head group. Based on the finding that at high lipid/peptide ratio the peptide induces unequal changes in the fluorescence parameters of phospholipid probes differing structurally only in their polar head groups, it is concluded that melittin induces lipid demixing in its nearest environment. Comparison of the fluorescence energy transfer from Trp to different lipid probes indicates that the depth of penetration of melittin into the bilayer depends on the polar head group composition of the phospholipid matrix and that certain segments of the melittin chain display a specific affinity for a given lipid head group.
通过测量肽的固有荧光、稳态荧光各向异性以及色氨酸荧光向同一磷脂荧光类似物的能量转移来研究蜂毒肽与由磷脂酰胆碱、鞘磷脂和磷脂酰丝氨酸或磷脂酰甘油组成的多组分脂质混合物的相互作用，这些磷脂荧光类似物在脂肪族链之一中带有蒽基乙烯基荧光团，与极性头部基团的距离各不相同。基于在高脂/肽比率下该肽会在结构上仅在极性头部基团上有所不同的磷脂探针的荧光参数中引起不平等变化这一发现，得出结论：蜂毒肽在其最邻近环境中诱导脂质分层。色氨酸向不同脂质探针的荧光能量转移的比较表明，蜂毒肽进入双层的穿透深度取决于磷脂基质的极性头部基团组成，并且蜂毒肽链的某些片段对给定的脂质头部基团表现出特定亲和力。
