水和乙醇的分层导致阳离子糖胺聚糖三肽的构象重新分布和凝胶化。
Demixing of water and ethanol causes conformational redistribution and gelation of the cationic GAG tripeptide.
作者信息
Milorey Bridget, Farrell Stefanie, Toal Siobhan E, Schweitzer-Stenner Reinhard
机构信息
Department of Chemistry, Drexel University, 3141 Chestnut Street, Philadelphia, PA, USA.
Department of Chemistry, University of Pennsylvania, 231, South 34th-Street, Philadelphia, PA 19104, USA.
出版信息
Chem Commun (Camb). 2015 Nov 28;51(92):16498-501. doi: 10.1039/c5cc06097d.
The cationic tripeptide GAG undergoes three conformational changes in binary mixtures of water and ethanol. At 17 mol% of ethanol conformational sampling is shifted from pPII towards β-strands. A more pronounced shift in the same direction occurs at 40 mol%. At ca. 55 mol% of ethanol and above a peptide concentration of ca. 0.2 M the ternary peptide-water-ethanol mixture forms a hydrogel which is comprised of unusually large crystalline like non-β sheet fibrils forming a sample spanning matrix.
阳离子三肽GAG在水和乙醇的二元混合物中会经历三种构象变化。在乙醇含量为17摩尔%时，构象采样从多聚脯氨酸II型向β-链转变。在40摩尔%时，会向相同方向发生更明显的转变。在乙醇含量约为55摩尔%及以上且肽浓度约为0.2 M时，三元肽-水-乙醇混合物形成一种水凝胶，它由异常大的类似晶体的非β片层纤维组成，形成一个贯穿样品的基质。
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