Vasilevskiĭ A A, Kozlov S A, Zhmak M N, Kudelina I A, Dubovskiĭ P V, Shaturskiĭ O Ia, Arsen'ev A S, Grishin E V
Bioorg Khim. 2007 Jul-Aug;33(4):405-12.
Analogues of latarcins Ltc1 and Ltc3b, antimicrobial peptides from the venom of the Central Asian spider Lachesana tarabaevi capable of formation of amphiphilic structures in membranes without involvement of disulfide bonds, were synthesized. The amino acid sequences of the analogues correspond to immature forms of these peptides, each of them containing an additional C-terminal amino acid residue. It is concluded from the study of the biological activity of the synthesized peptides that the posttranslational C-terminal amidation of Ltc3b is a functionally important modification that ensures a high activity of the mature peptide. The lipid composition was shown to affect the interaction of synthesized peptides with artificial membranes. The analogue of Ltc3b manifested the highest activity on cholesterol-containing membranes. The mechanism of action of the studied antimicrobial peptides on membranes is discussed.
合成了来自中亚蜘蛛Lachesana tarabaevi毒液的抗菌肽latarcins Ltc1和Ltc3b的类似物,这些抗菌肽能够在不涉及二硫键的情况下在膜中形成两亲结构。类似物的氨基酸序列对应于这些肽的未成熟形式,每个都含有一个额外的C末端氨基酸残基。从合成肽的生物活性研究得出结论,Ltc3b的翻译后C末端酰胺化是一种功能上重要的修饰,可确保成熟肽具有高活性。研究表明脂质组成会影响合成肽与人工膜的相互作用。Ltc3b的类似物在含胆固醇的膜上表现出最高活性。讨论了所研究的抗菌肽对膜的作用机制。