Peptide profile of human acquired enamel pellicle using MALDI tandem MS

• Tipo: Artigo em Revista Científica Internacional
• Data: 2008

Autores

vitorino, r (Autor) Outra; calheiros-lobo, mj (Autor) Outra; duarte, ja (Autor) FADEUP; domingues, pm (Autor) Outra; amado, fml (Autor) Outra

Revista

Título: Journal of Separation Science

Vol. 31 Nº 3

Páginas: 523-537

ISSN: 1615-9306

Editora: Wiley-Blackwell

Indexação

ISI Web of Knowledge - 32 Citações

Scopus - 35 Citações

Pubmed / Medline

Classificação Científica

FOS: Ciências exactas e naturais > Química

Outras Informações

ID Authenticus: P-004-1VV

DOI: 10.1002/jssc.200700486

Abstract (EN): The present study proposes a strategy for human in vivo acquired enamel pellicle (AEP) peptidome characterisation based on sequential extraction with guanidine and TEA followed by MALDI-TOF/TOF identification. Three different nanoscale analytical approaches were used: samples were subjected to tryptic digestion followed by nano-HPLC and mass spectrometry (MS and MS/MS) analysis. Undigested samples were analysed by LC-MS (both linear and reflector modes) and LC-MS/MS analysis, and samples were subjected to nano-HPLC followed by on-plate digestion and mass spectrometry (MS and MS/MS) analysis. The majority of the identifications corresponded to peptide/protein fragments of salivary protein, belonging to the classes: acidic PRPs, basic PRPs, statherin, cystatins S and SN and histatin 1 (all also identified in intact form). Overall, more than 90 peptides/proteins were identified. Results clearly show that peptides with acidic groups are enriched in the TFA fraction while peptides with no acidic or phosphate groups are prevalent on the guanidine extract. Also, phosphorylated peptides were observed mainly on the TFA fraction. Fragments present in the AEP show a predominance of cleavage points located at Arg, Tyr and Lys residues. Obtained data suggest that proteolytic activity could influence AEP formation and composition.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 15