Wieprecht T, Dathe M, Krause E, Beyermann M, Maloy W L, MacDonald D L, Bienert M
Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.
FEBS Lett. 1997 Nov 3;417(1):135-40. doi: 10.1016/s0014-5793(97)01266-0.
Starting from the sequences of magainin 2 analogs, peptides with slightly increased hydrophobic moment (mu) but retained other structural parameters were designed. Circular dichroism investigations revealed that all peptides adopt an alpha-helical conformation when bound to phospholipid vesicles. Analogs with increased mu were considerably more active in permeabilizing vesicles mainly composed of zwitterionic lipid. In addition, the antibacterial and hemolytic activities of these analogs were enhanced. Correlation of permeabilization and binding indicated that the activity increase is predominantly caused by an increased membrane affinity of the peptides due to strengthened hydrophobic interactions.
从马盖宁2类似物的序列出发，设计了疏水矩（μ）略有增加但保留其他结构参数的肽。圆二色性研究表明，所有肽在与磷脂囊泡结合时均采用α-螺旋构象。μ增加的类似物在使主要由两性离子脂质组成的囊泡通透方面活性显著更高。此外，这些类似物的抗菌和溶血活性增强。通透作用与结合的相关性表明，活性增加主要是由于疏水相互作用增强导致肽与膜的亲和力增加所致。
