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Issue 26, 2019
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A novel mass spectrometry-cleavable, phosphate-based enrichable and multi-targeting protein cross-linker

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Abstract

Chemical cross-linking mass spectrometry (XL-MS) is a powerful technology for obtaining protein structural information and studying protein–protein interactions. We report phospho-bisvinylsulfone (pBVS) as a novel water-soluble, MS-cleavable, phosphate-based enrichable and multi-targeting cross-linker. In this approach, the fragmentation of pBVS cross-linked peptides occurs in situ through retro-Michael addition. The phosphate group is successfully used as a small affinity tag to isolate cross-linked peptides from the highly abundant non-cross-linked peptides. In addition, the linker targets multiple types of amino acid residues, including cysteine, lysine and histidine. This method was applied to cross-link bovine serum albumin (BSA), myoglobin and Lbcpf1 demonstrating the ability to yield accurate and abundant information to facilitate protein structure elucidation.

Graphical abstract: A novel mass spectrometry-cleavable, phosphate-based enrichable and multi-targeting protein cross-linker

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Publication details

The article was received on 21 Feb 2019, accepted on 23 May 2019 and first published on 23 May 2019


Article type: Edge Article
DOI: 10.1039/C9SC00893D
Chem. Sci., 2019,10, 6443-6447
  • Open access: Creative Commons BY-NC license
    All publication charges for this article have been paid for by the Royal Society of Chemistry

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    A novel mass spectrometry-cleavable, phosphate-based enrichable and multi-targeting protein cross-linker

    R. Huang, W. Zhu, Y. Wu, J. Chen, J. Yu, B. Jiang, H. Chen and W. Chen, Chem. Sci., 2019, 10, 6443
    DOI: 10.1039/C9SC00893D

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