Adsorption-induced conformational changes of α-helical peptides
Adsorption-induced conformational changes of α-helical peptides
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DOI：
10.1021/la010156s
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发表时间：
2001-08-07
期刊：
影响因子：
3.9
通讯作者：
Read, MJ
中科院分区：
文献类型：
--
作者：
Burkett, SL;Read, MJ
在水溶液中，具有α-螺旋结构的肽被吸附到阴离子和阳离子胶态二氧化硅基底上，并通过H-1 NMR和圆二色性研究了吸附肽的取向和构象。由天冬氨酸、丙氨酸和精氨酸片段组成的肽吸附到带电的胶体二氧化硅上，使得带互补电荷的氨基酸侧链与基底表面相邻。稳定α-螺旋结构的分子内相互作用受到吸附时建立的分子间相互作用的干扰，并且肽在吸附到基底表面后发生构象变化。部分螺旋度损失从一个或两个肽末端传播，尽管吸附的分子保留一些α-螺旋结构。
Peptides that have a-helical structures in solution have been adsorbed to anionic and cationic colloidal silica substrates in aqueous solution, and the orientation and conformation of the adsorbed peptides have been studied by H-1 NMR and circular dichroism. The peptides, which are composed of aspartate, alanine, and arginine segments, adsorb to charged colloidal silica such that the complementary-charged amino acid side chains are adjacent to the substrate surface. The intramolecular interactions that stabilize the a-helical structure are perturbed by the intermolecular interactions established upon adsorption, and the peptides undergo a conformational change upon adsorption to the substrate surface. Partial helicity loss propagates from one or both of the peptide termini, although the adsorbed molecules retain some a-helical structure.