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温度诱导弹性蛋白样肽 GVG(VPGVG)构象变化。

Temperature induced conformational changes in the elastin-like peptide GVG(VPGVG).

机构信息

Institut für Festkörperphysik, Technische Universität Darmstadt, Hochschulstraße 6, 64289 Darmstadt, Germany.

出版信息

Soft Matter. 2019 May 22;15(20):4192-4199. doi: 10.1039/c9sm00583h.

DOI:10.1039/c9sm00583h
PMID:31065653
Abstract

Elastin-like peptides are biopolymers that display LCST behaviour in solution quite similar to other synthetic polymers like polyethylene oxide. Here we study the structure of the peptide GVG(VPGVG)3 in a temperature range of 25 °C to 70 °C with small angle neutron scattering. The LCST for this peptide is outside the experimental range of temperatures. Molecular conformation is well described within the model of a random coil but increasing temperature leads to significant changes. The peptide displays a combination of conformational change and aggregation that show up in the scattering at low and intermediate scattering vector q. The aggregate size is determined from an integral measure of the scattered intensity. It increases with temperature and concentration. For low concentration we find a size variation with temperature that may be related to the collapse of conformation at the inverse temperature transition (ITT).

摘要

弹性蛋白样肽是一种生物聚合物,在溶液中的 LCST 行为与其他合成聚合物(如聚氧化乙烯)非常相似。在这里,我们使用小角中子散射技术研究了温度范围在 25°C 至 70°C 之间的肽 GVG(VPGVG)3 的结构。该肽的 LCST 超出了实验温度范围。在无规线团模型中,分子构象得到了很好的描述,但随着温度的升高,会发生显著的变化。该肽表现出构象变化和聚集的组合,在低和中等散射矢量 q 处的散射中表现出来。聚集尺寸是通过对散射强度的积分测量来确定的。它随温度和浓度的增加而增加。对于低浓度,我们发现温度变化的尺寸变化可能与逆温度转变 (ITT) 时构象的崩溃有关。

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