Tryptophan-specific peptide modification through metal-free photoinduced N-H alkylation employing N-aryl glycines

Tryptophan (Trp) carries a unique heteroaromatic indole side chain and plays a critical role in peptide or protein modification. Herein, we have reported a metal-free photoinduced N-H alkylation strategy using N-aryl glycines for specific modification of tryptophan-containing peptides. The robustnes...

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Veröffentlicht in:Chinese chemical letters Jg. 35; H. 6; S. 109244 - 319
Hauptverfasser: Yin, Jianhui, Huang, Wenjing, Guo, Changyong, Liu, Chao, Gao, Fei, Hu, Honggang
Format: Journal Article
Sprache:Englisch
Veröffentlicht: Elsevier B.V 01.06.2024
School of Medicine or Institute of Translation Medicine,Shanghai University,Shanghai 200444,China
Schlagworte:
Glycine
Modification
Peptide
Photoinduced
Tryptophan
Tryptophan
Modification
Glycine
Peptide
Photoinduced
ISSN:1001-8417, 1878-5964
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Zusammenfassung:Tryptophan (Trp) carries a unique heteroaromatic indole side chain and plays a critical role in peptide or protein modification. Herein, we have reported a metal-free photoinduced N-H alkylation strategy using N-aryl glycines for specific modification of tryptophan-containing peptides. The robustness of our approach is demonstrated by its wide substrate scope, excellent isolated yields, as well as almost unobservable side effects. Using this highly efficiently metal-free condition, alkylated Trp-containing peptides can be smoothly assembled. This study provides a reliable and practical tool for the chemo-selective modification of various tryptophan containing oligopeptides. Various alkylated Trp-containing peptides were synthesized by metal-free photoinduced decarboxylative alkylation in acceptable to excellent yields. [Display omitted]
ISSN:1001-8417
1878-5964
DOI:10.1016/j.cclet.2023.109244