Mass Spectrometric Detection of Affinity Purified Crosslinked Peptides

Overview

Journal J Am Soc Mass Spectrom

Specialty Chemistry

Date 2004 May 18

PMID 15144972

Citations 24

Authors

Gregory B Hurst

Trish K Lankford

Stephen J Kennel

Affiliations

Soon will be listed here.

Abstract

Chemical crosslinking of proteins combined with mass spectrometric analysis of the tryptic digest of the products shows considerable promise as a tool for interrogating structure and geometry of proteins and protein complexes. An impediment to the use of this tool has been the difficulty of distinguishing crosslinked peptide pairs from non-crosslinked peptides, and from the products of side reactions. We describe the use of a commercially available biotinylated crosslinking reagent, sulfo-SBED, that allows affinity-based enrichment of crosslinked species. An intramolecular crosslink is prepared using the peptide neurotensin as a model system. Matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectra show the predicted crosslinking product, as well as several side products. Finally, we describe the optimized enrichment of biotinylated species, and reduction of non-specific binding, for a batch-mode affinity separation based on immobilized monomeric avidin.

Citing Articles

Quantitative Cross-Linking of Proteins and Protein Complexes.

Barth M, Schmidt C Methods Mol Biol. 2021; 2228:385-400.

PMID: 33950504 DOI: 10.1007/978-1-0716-1024-4_26.

Chemical cross-linking in the structural analysis of protein assemblies.

Chu F, Thornton D, Nguyen H Methods. 2018; 144:53-63.

PMID: 29857191 PMC: 6051896. DOI: 10.1016/j.ymeth.2018.05.023.

Development of Large-scale Cross-linking Mass Spectrometry.

Barysz H, Malmstrom J Mol Cell Proteomics. 2017; 17(6):1055-1066.

PMID: 28389583 PMC: 5986251. DOI: 10.1074/mcp.R116.061663.

Comprehensive Cross-Linking Mass Spectrometry Reveals Parallel Orientation and Flexible Conformations of Plant HOP2-MND1.

Rampler E, Stranzl T, Orban-Nemeth Z, Hollenstein D, Hudecz O, Schlogelhofer P J Proteome Res. 2015; 14(12):5048-62.

PMID: 26535604 PMC: 6207341. DOI: 10.1021/acs.jproteome.5b00903.

Identification of the components of a glycolytic enzyme metabolon on the human red blood cell membrane.

Puchulu-Campanella E, Chu H, Anstee D, Galan J, Tao W, Low P J Biol Chem. 2012; 288(2):848-58.

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