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On-target deuteration for peptide sequencing by laser mass spectrometry

✍ Scribed by Bernhard Spengler; Frank Lützenkirchen; Raimund Kaufmann

Publisher
John Wiley and Sons
Year
1993
Tongue
English
Weight
664 KB
Volume
28
Category
Article
ISSN
1076-5174

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✦ Synopsis

Hydrogen-deuterium exchange was evaluated as a tool for sequence analysis of peptides by matrix-assisted laser desorption-ionization utilizing post-source decay (PSD-MALDI). The number of exchangeable hydrogens (EH) of precursor ions and product ions can be determined from the mass difference between ion signals originating from the deuterated and the non-deuterated form of a peptide, resulting in a second dimension of structural information. The reliability of sequence determination by combinatorial algorithms or pattern recognition techniques is considerably increased by employng this 'EH spectroscopy.' On-target deuteration is a simple preparatory step which can be performed reversibly with the already mass-analysed sample within a few minutes and without consumption of additional sample material. The efficiency of hydrogen-deuterium exchange with this technique is about 98.5%. In addition to supporting sequence analysis, deuteration can be used to investigate fundamental fragmentation mechanisms of peptides in PSD-MALDI. Inconsistencies with expected fragmentation pathways have been found for fragments a,-a3 of substance P.

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