Review article

Sequence Determination of Pharmaceutical Peptides by MALDI-TOF Tandem Mass Spectrometry

Mario Cindrić ; Ruđer Bošković Institute, Division of Molecular Medicine, Zagreb, Croatia
Mirela Sedić ; Ruđer Bošković Institute, Division of Molecular Medicine, Zagreb, Croatia
Anita Horvatić ; Ruđer Bošković Institute, Division of Molecular Medicine, Zagreb, Croatia
Ivana Dodig ; Ruđer Bošković Institute, Division of Molecular Medicine, Zagreb, Croatia

Abstract

Although the peptide ion mechanisms of pre-dissociation, dissociation and post-dissociation have been well-studied over the past fifteen years, their practical application still has to be implemented into modern mass spectrometry-driven proteomics and bioanalysis. Unambiguous peptide sequence determination by mass spectrometry relies on the idea that only one continuous series of ions in mass spectrum can assure full sequence determination and meets the requirements of peptide analysis quality. This set of rules defined for the peptide analysis by tandem mass spectrometry would generally improve an overall reliability and data accuracy. Based on the process mechanisms of gas-phase peptide bond dissociation, a relatively small and large model peptides are unambiguously analyzed (bivalirudin and exenatide) showing that derivatization concepts of the C- or N-terminus derivatization (SPITC and Lys-tag) can be avoided.

Keywords

MALDI-TOF/TOF; sequence determination; pharmaceutical peptide; bivalirudin; exenatide

Hrčak ID:

63153

URI

https://hrcak.srce.hr/63153

Publication date:

15.12.2010.

Article data in other languages: croatian

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