Peptides comprising many hydrophobic amino acids are almost insoluble under physiological buffer conditions, which complicates their structural analysis. To investigate the three-dimensional structure of the hydrophobic leucinostatin derivative ZHAWOC6027, the previously developed host lattice display technology was applied. Two designed ankyrin-repeat proteins (DARPins) recognizing a biotinylated ZHAWOC6027 derivative were selected from a diverse library by ribosome display under aqueous buffer conditions. ZHAWOC6027 was immobilized by means of the DARPin in the host lattice and the structure of the complex was determined by X-ray diffraction. ZHAWOC6027 adopts a distorted α-helical conformation. Comparison with the structures of related compounds that have been determined in organic solvents reveals elevated flexibility of the termini, which might be functionally important.

中文翻译：

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通过主晶格显示确定疏水性亮氨酸抑制素衍生物的结构

包含许多疏水性氨基酸的肽在生理缓冲条件下几乎不溶，这使其结构分析复杂化。为了研究疏水亮氨酸抑制素衍生物 ZHAWOC6027 的三维结构，应用了先前开发的主晶格显示技术。在水缓冲条件下通过核糖体展示从多样化的文库中选择识别生物素化 ZHAWOC6027 衍生物的两种设计的锚蛋白重复蛋白 (DARPins)。ZHAWOC6027 通过主晶格中的 DARPin 固定，并通过 X 射线衍射确定复合物的结构。ZHAWOC6027采用扭曲的α-螺旋构象。与已在有机溶剂中确定的相关化合物的结构进行比较，揭示了末端灵活性的提高，