科研之友
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摘要
Disulfide bond formation is a common mechanism for regulating conformational changes in proteins during oxidative folding. Despite extensive studies of the use of multiple disulfide bonds to constrain peptide conformation, few studies have explored their usage in developing self‐assembling peptides. Herein, we report that a thiol‐rich peptide could fold into an amphiphilic β‐hairpin conformation through the formation of two hetero‐disulfide bonds upon oxidation, subsequently self‐assembling into a mechanically rigid hydrogel. Breaking disulfide bonds under reductive condition, the hydrogel exhibited a transition from hydrogel to solution. Molecular simulation revealed that intermolecular interaction between two tryptophan residues was indispensable for hydrogelation. This work is the first case of the use of multiple disulfide bonds to control conformational change and self‐assembly, and provides a cell‐compatible hydrogel material for potential biomedical application.(#br)Disulfide bond formation is usually used in nature for the regulation and stabilization of protein conformations. This principle has now been expanded to control the conformational change of thiol‐rich peptides into an amphiphilic β‐hairpin conformation, which undergoes a subsequent self‐assembly to form a mechanically rigid hydrogel. Such a stimuli‐responsive feature allows the biomedical application of such peptides.
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单位固体表面物理化学国家重点实验室
