Peptide profile of human acquired enamel pellicle using MALDI tandem MS

• Type: Article in International Scientific Journal
• Date: 2008

Authors

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

Journal

Title: Journal of Separation Science

Vol. 31 No. 3

Pages: 523-537

ISSN: 1615-9306

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 32 Citations

Scopus - 35 Citations

Pubmed / Medline

Scientific classification

FOS: Natural sciences > Chemical sciences

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 15