Peptides containing selenocysteine moieties are susceptible to non‐catalytic reactions of diselenide bonds metathesis induced by visible light. In contrast to previously reported radical metathesis of disulfide bridges in cysteine derivatives, this newly developed reaction is fast and clean, and proceeds without decomposition of peptides and without formation of side products. The diselenide bond in peptides was reported in literature to be more stable than the disulfide one and also less susceptible to metathesis induced by thiols and reducing reagents. We demonstrated that visible light induces fast metathesis of Se−Se bonds in peptides. This reaction is important for the folding of peptides containing selenocysteine residues and may find application in designing dynamic combinatorial libraries of peptides responsive to external influence.

中文翻译：

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肽中的光驱动二硒代分解。

含有硒代半胱氨酸部分的肽易受可见光诱导的二硒键复分解的非催化反应的影响。与先前报道的半胱氨酸衍生物中二硫键的自由基复分解相反，该新开发的反应快速，干净，并且进行过程中不会分解肽，也不会形成副产物。已有文献报道，肽中的二硒键比二硫键更稳定，而且对硫醇和还原剂诱导的复分解反应较不敏感。我们证明了可见光诱导了肽中Se-Se键的快速复分解。该反应对于折叠含有硒代半胱氨酸残基的肽很重要，并且可以在设计响应外部影响的肽的动态组合文库中找到应用。