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

Yingqian Zhang, Chuanlong Zang, Guoce An, Mengdi Shang, Zenghui Cui, Gong Chen, Zhen Xi and Chuanzheng Zhou ()
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Yingqian Zhang: Nankai University
Chuanlong Zang: Nankai University
Guoce An: Criminal Investigation Police University of China
Mengdi Shang: Nankai University
Zenghui Cui: Nankai University
Gong Chen: Nankai University
Zhen Xi: Nankai University
Chuanzheng Zhou: Nankai University

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract 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 reagents for cysteine-specific protein modification. These compounds can be facilely synthesized via a one-pot mild reaction and they show comparable tagging efficiency but higher cysteine specificity than the maleimide counterparts. The addition of cysteine to 3Br-5MPs generates conjugates that are amenable to secondary addition by another thiol or cysteine, making 3Br-5MPs valuable for multi-functionalization of a single cysteine and disulfide bridging bioconjugation. The labeling reaction and subsequent treatments are mild enough to produce stable and active protein conjugates for biological applications.

Date: 2020
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DOI: 10.1038/s41467-020-14757-4

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