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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Yingqian Zhang & Chuanlong Zang & Guoce An & Mengdi Shang & Zenghui Cui & Gong Chen & Zhen Xi & Chuanzheng Zhou, 2020. "Cysteine-specific protein multi-functionalization and disulfide bridging using 3-bromo-5-methylene pyrrolones," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14757-4
    DOI: 10.1038/s41467-020-14757-4
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