Cysteine-specific protein multi-functionalization and disulfide bridging using 3-bromo-5-methylene pyrrolones

• Published in: Nature communications Vol. 11; no. 1; pp. 1015 - 10
• Main Authors: Zhang, Yingqian, Zang, Chuanlong, An, Guoce, Shang, Mengdi, Cui, Zenghui, Chen, Gong, Xi, Zhen, Zhou, Chuanzheng
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 21.02.2020; Nature Publishing Group; Nature Portfolio
• Subjects: 140/131; 140/58; 639/638/403/933; 639/638/549/933; 639/638/92/469; 82/16; 82/29; Bridging; Chemistry Techniques, Synthetic - methods; Conjugates; Cysteine; Cysteine - chemistry; Disulfides - chemistry; Humanities and Social Sciences; Indicators and Reagents - chemistry; Methylene; multidisciplinary; Organic Chemistry Phenomena; Proteins; Proteins - chemistry; Pyrroles - chemistry; Reagents; Robustness; Science; Science (multidisciplinary); Somatostatin - chemistry

Many reagents have been developed for cysteine-specific protein modification. However, few of them allow for multi-functionalization of a single Cys residue and disulfide bridging bioconjugation. Herein, we report 3-bromo-5-methylene pyrrolones (3Br-5MPs) as a simple, robust, and versatile class of...