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首页> 外文期刊>Biochemistry >Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives(,).
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Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives(,).

机译：Tachyples I及其活性芳族线性衍生物（，）的溶液和胶束结合结构。

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摘要

Tachyplesin I is a 17-residue peptide isolated from the horseshoe crab, Tachyplesus tridentatus.It has high antimicrobial activity and adopts a beta-hairpin conformation in solution stabilized by two cross-strand disulfide bonds. We report an NMR structural investigation of wild-type tachyplesin I and three linear derivatives (denoted TPY4, TPF4, and TPA4 in which the bridging cysteine residues are uniformly replaced with tyrosine, phenylalanine, and alanine, respectively). The three-dimensional aqueous solution structures of the wild type and the active variant TPY4 reveal very similar beta-hairpin conformations. In contrast, the inactive variant TPA4 is unstructured in solution. The arrangement of the tyrosine side chains in the TPY4 structure suggests that the beta-hairpin is stabilized by aromatic ring stacking interactions. This is supported by experiments in which the beta-hairpin structure of TPF4 is disrupted by the addition of phenol, but not by the addition of an equimolar amount of cyclohexanol. We have also determined the structures of wild-type tachyplesin I and TPY4 in the presence of dodecylphosphocholine micelles. Both peptides undergo significant conformational rearrangement upon micelle association. Analysis of the micelle-associated peptide structures shows an increased level of exposure of specific hydrophobic side chains and an increased hydrophobic integy moment. Comparison of the structures in micelle and aqueous solution for both wild-type tachyplesin I and TPY4 reveals two requirements for high antimicrobial activity: a beta-hairpin fold in solution and the ability to rearrange critical side chain residues upon membrane association.
机译：TachypleSI是从马蹄蟹分离的17-残基肽，TachypleSus Tridentatus.it具有高抗微生物活性，并采用由两个十字链二硫键稳定的溶液中的β-发夹构象。我们报告了对野生型TachypleSI和三种线性衍生物的NMR结构研究（表示TPY4，TPF4和TPA4，其中桥接半胱氨酸残基分别均匀地用酪氨酸，苯丙氨酸和丙氨酸替换）。野生型和活性变体TPY4的三维水溶液结构揭示了非常相似的β-发夹构象。相反，无效变体TPA4在溶液中非结构。 Tyrosine侧链在TPy4结构中的布置表明β-发夹通过芳香环堆叠相互作用稳定。这是通过实验支持的，其中TPF4的β-发夹结构通过添加苯酚而破坏，但不是添加等摩尔的环己醇。在十二烷基磷胶胶束存在下，我们还确定了野生型TachypleSI和TPY4的结构。两种肽在胶束协会后经历显着的构象重新排列。胶束相关肽结构的分析显示特异性疏水侧链的暴露水平和增加的疏水性整体矩。胶束和水溶液中的结构的比较野生型TachyplesI和TPY4揭示了对高抗微生物活性的两个要求：β-发夹折叠溶液和重新排列膜结合的临界侧链残基的能力。

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