Saberwal G, Nagaraj R
Centre for Cellular and Molecular Biology, Hyderabad, India.
Biochim Biophys Acta. 1989 Sep 18;984(3):360-4. doi: 10.1016/0005-2736(89)90303-9.
Peptides corresponding to the amino terminal region of pardaxin from Pardachirus pavoninus (Gly-Phe-Phe-Ala-Leu-Ile-Pro-Lys-Ile-Ile-Ser-Ser-Pro-Leu-Phe) have been synthesized and their interaction with model membranes of phosphatidyl choline and serine studied by 90 degrees C light scattering and fluorescence spectroscopy. The amino terminal 8-residue peptide and the protected 15-residue peptide cause only aggregation of lipid vesicles. The deprotected 15-residue peptide has the ability to cause aggregation and release of entrapped carboxyfluorescein with both phosphatidyl choline and serine lipid vesicles, like pardaxin. The membrane-perturbing ability of the amino terminal 15-residue peptide can be attributed to its ability to adopt an alpha-helical conformation which is amphiphilic in nature in a hydrophobic environment.
已合成了与孔雀斑鳐（Pardachirus pavoninus）豹蟾鱼毒素氨基末端区域相对应的肽（甘氨酸 - 苯丙氨酸 - 苯丙氨酸 - 丙氨酸 - 亮氨酸 - 异亮氨酸 - 脯氨酸 - 赖氨酸 - 异亮氨酸 - 异亮氨酸 - 丝氨酸 - 丝氨酸 - 脯氨酸 - 亮氨酸 - 苯丙氨酸），并通过90℃光散射和荧光光谱研究了它们与磷脂酰胆碱和丝氨酸模型膜的相互作用。氨基末端8个残基的肽和受保护的15个残基的肽仅导致脂质囊泡聚集。脱保护的15个残基的肽具有导致磷脂酰胆碱和丝氨酸脂质囊泡聚集并释放包封的羧基荧光素的能力，类似于豹蟾鱼毒素。氨基末端15个残基的肽的膜扰动能力可归因于其在疏水环境中形成两亲性α-螺旋构象的能力。
