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Article Dans Une Revue Journal of The American Society for Mass Spectrometry Année : 2011

Sequencing Lys-N Proteolytic Peptides by ESI and MALDI Tandem Mass Spectrometry

Résumé

In this study, we explored the MS/MS behavior of various synthetic peptides that possess a lysine residue at the N-terminal position. These peptides were designed to mimic peptides produced upon proteolysis by the Lys-N enzyme, a metalloendopeptidase issued from a Japanese fungus Grifola Frondosa that was recently investigated in proteomic studies as an alternative to trypsin digestion since a specific cleavage at the amide X-Lys chain is obtained providing N-terminal lysine peptide fragments. In contrast to tryptic peptides exhibiting a In lysine or arginine residues solely at the C-terminal position, and thus devoid of such basic amino acids within the sequence, these Lys-N proteolytic peptides can contain the highly basic arginine residue anywhere within the peptide chain. The fragmentation patterns of such sequences with ESI-QqTof and MALDI-Tof/Tof mass spectrometers commonly used in proteomic bottom-up experiments were investigated.

Domaines

Chimie organique
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Dates et versions

hal-00580756 , version 1 (29-03-2011)

Identifiants

Citer

Mathieu Dupré, Sonia Cantel, Pascal Verdié, Jean Martinez, Christine Enjalbal. Sequencing Lys-N Proteolytic Peptides by ESI and MALDI Tandem Mass Spectrometry. Journal of The American Society for Mass Spectrometry, 2011, 22, pp.265-279. ⟨10.1007/s13361-010-0022-7⟩. ⟨hal-00580756⟩
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