Optimizing the enrichment of cross-linked products for mass spectrometric protein analysis

Rapid Communications in Mass Spectrometry : RCM
Romy FritzscheAndrea Sinz

Abstract

Chemical cross-linking in combination with a mass spectrometric analysis of the created cross-linked products is an area of growing interest for deriving low-resolution structural information of proteins and protein complexes. One of the greatest challenges is the complexity of the created cross-linking mixtures, which can be met by a charge-based enrichment of cross-linked peptides after proteolytic digestion using strong cation-exchange (SCX) chromatography. SCX chromatography was used for the enrichment of cross-linked peptides with the N-hydroxysuccinimide ester bis(sulfosuccinimidyl)succinate (BS(3)) prior to a mass spectrometric analysis by nano-HPLC/nano-ESI-LTQ-Orbitrap-MS/MS. Bovine serum albumin (BSA) and glutathione S-transferase (GST) were employed as model proteins. Conditions for SCX enrichment were optimized for obtaining as many interpeptide cross-linked peptides as possible in order to maximize the amount of structural information from a single experiment. With an SCX-based enrichment step of cross-linked products within BSA using the cross-linker BS(3), 154 interpeptidal cross-linking products were identified during nano-HPLC/nano-ESI-MS/MS analyses, whereas analyses without a prior SCX enrichment allowed the ...Continue Reading

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Citations

May 31, 2012·Analytical and Bioanalytical Chemistry·Jens SproßAndrea Sinz
May 23, 2012·Analytical and Bioanalytical Chemistry·Cordula KlockenbuschJuergen Kast
Aug 7, 2013·Journal of Structural and Functional Genomics·Eric D MerkleyJoshua N Adkins
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Oct 2, 2019·ACS Central Science·Barbara SteigenbergerRichard A Scheltema
Feb 23, 2019·Journal of Proteome Research·Zixiang FangSaiful M Chowdhury

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