Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif.
Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif.
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DOI：
10.1021/jacs.5b07206
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发表时间：
2015-09-23
影响因子：
15
通讯作者：
Gellman SH
中科院分区：
文献类型：
--
作者：
Hayouka Z;Thomas NC;Mortenson DE;Satyshur KA;Weisblum B;Forest KT;Gellman SH
准外消旋晶体学已被用于探索一组宿主防御肽衍生物中的同手性和异手性缔合的意义。先前报道的爪蟾抗菌肽2衍生物的外消旋晶体结构显示出具有“苯丙氨酸拉链”的同手性二聚体缔合，该“苯丙氨酸拉链”显著地具有苯丙氨酸在介导二聚化和形成暴露的疏水条带中的双重作用。在两种新的准消旋体中也可以看到这种基序，它们含有爪蟾抗菌肽2衍生物的D型沿着L肽，其中一个Ala被β-氨基酸残基取代。这种结构趋势支持了Phe拉链基序具有功能意义的假设。
Quasiracemic crystallography has been used to explore the significance of homochiral and heterochiral associations in a set of host-defense peptide derivatives. The previously reported racemic crystal structure of a magainin 2 derivative displayed a homochiral dimer association featuring a “phenylalanine zipper” notable for the dual roles of phenylalanines in mediating dimerization and formation of an exposed hydrophobic swath. This motif is seen as well in two new quasiracemate crystals that contain the D form of the magainin 2 derivative along with an L-peptide in which one Ala has been replaced by a β-amino acid residue. This structural trend supports the hypothesis that the Phe zipper motif has functional significance.