A Reductive Trigger for Peptide Self-Assembly and Hydrogelation
A Reductive Trigger for Peptide Self-Assembly and Hydrogelation
复制标题
DOI：
10.1021/ja1025535
复制
发表时间：
2010-07-21
影响因子：
15
通讯作者：
Nilsson, Bradley L.
中科院分区：
文献类型：
--
作者：
Bowerman, Charles J.;Nilsson, Bradley L.
刺激反应性多肽的自组装为控制环境的自组装提供了一种强有力的方法。本文描述了用于肽自组装和随后的水凝胶的还原触发器的发展。一个自组装肽序列Ac-C(FKFE)(2)CG-NH2通过侧翼半胱氨酸残基的二硫键被环化。这种多肽的大环形式实施了构象限制，阻止了自组装所需的β-折叠构象的采用。一旦二硫键被还原，多肽就松弛成首选的β-折叠构象，并立即自组装成纤维状超结构。在足够的多肽浓度下，自组装伴随着刚性、粘弹性水凝胶的形成。
Stimulus-responsive peptide self-assembly provides a powerful method for controlling self-assembly as a function of environment. The development of a reductive trigger for peptide self-assembly and subsequent hydrogelation is described herein. A self-assembling peptide sequence, Ac-C(FKFE)(2)CG-NH2, was cyclized via disulfide bonding of the flanking cysteine residues. The macrocyclic form of this peptide enforces a conformational restraint that prevents adoption of the beta-sheet conformation that is required for self-assembly. Upon reduction of this disulfide bond, the peptide relaxes into the preferred beta-sheet conformation, and immediate self-assembly into fibrillar superstructures occurs. At sufficient peptide concentration, self-assembly is accompanied by the formation of rigid, viscoelastic hydrogels.