Fragmentation features of intermolecular cross-linked peptides using N-hydroxy-succinimide esters by MALDI- and ESI-MS/MS for use in structural proteomics

Author(s)

Santos, Luiz F. A. ^{[1, 2]} ; Iglesias, Amadeu H. ^{[1, 2]} ; Gozzo, Fabio C. ^{[1, 2]}

Affiliation

^[1] Univ Estadual Campinas, Inst Chem, BR-13083970 Campinas, SP - Brazil

^[2] Inst Nacl Ciencia & Tecnol Bioanalit, BR-13083970 Campinas, SP - Brazil

• Document type: Journal article
• Source: Journal of Mass Spectrometry; v. 46, n. 8, p. 742-750, AUG 2011.
• Web of Science Citations: 9

Abstract

The use of mass spectrometry coupled with chemical cross-linking of proteins has become one of the most useful tools for proteins structure and interactions studies. One of the challenges in these studies is the identification of the cross-linked peptides. The interpretation of the MS/MS data generated in cross-linking experiments using N-hydroxy succinimide esters is not trivial once a new amide bond is formed allowing new fragmentation pathways, unlike linear peptides. Intermolecular cross-linked peptides occur when two different peptides are connected by the cross-linker and they yield information on the spatial proximity of different domains (within a protein) or proteins (within a complex). In this article, we report a detailed fragmentation study of intermolecular cross-linked peptides, generated from a set of synthetic peptides, using both ESI and MAID! to generate the precursor ions. The fragmentation features observed here can be helpful in the interpretation and identification of cross-linked peptides present in cross-linking experiments and be further implemented in search engine's algorithms. Copyright (C) 2011 John Wiley \& Sons, Ltd. (AU)

• FAPESP's process: 08/57805-2 - Institute of Bioanalytics
• Grantee: Lauro Tatsuo Kubota
• Support Opportunities: Research Projects - Thematic Grants