Peptidomic analysis of human acquired enamel pellicle

• Type: Article in International Scientific Journal
• Date: 2007

Authors

vitorino, r (Author) Other; calheiros-lobo, mj (Author) Other; williams, j (Author) Other; ferrer-correia, aj (Author) Other; tomer, kb (Author) Other; duarte, ja (Author) FADEUP; domingues, pm (Author) Other; amado, fm (Author) Other

Journal

Title: Biomedical Chromatography

Vol. 21 No. 1

Pages: 1107-1117

ISSN: 0269-3879

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 34 Citations

Scopus - 38 Citations

Pubmed / Medline

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-004-6D7

DOI: 10.1002/bmc.830

Abstract (EN): Human acquired enamel pellicle is the result of a selective interaction of salivary proteins and peptides with the tooth surface. In the present work, the characterization of the peptides as well as the type of interactions established with the enamel surface was performed. Peptides from in vivo bovine enamel implants in the human oral cavity were sequentially extracted using guanidine and trifluoroacetic acid solutions and the fractions obtained were analysed by LC-MS and LC-MS/MS. Based on the LC-MS data, six phosphorylated peptides were identified in an intact form, strongly adsorbed to the enamel surface. Data from the LC-MS/MS analyses allowed us to identified 30 fragment peptides non-covalently bonded to enamel [basic proline-rich proteins, histatins (I and 3) and acidic proline-rich protein classes]. The tandem mass spectrometry experiments showed the existence of a pattern of amide bond cleavage for the different identified peptide classes suggesting a selective proteolytic activity. For histatins, a predominance of cleavage at Arg, Lys and His residues was observed, while for basic proline-rich proteins, cleavage at Arg and Pro residues prevailed. In the case of acidic proline-rich proteins, a clearly predominance of cleavage of the Gln-Gly amide bond was evident. Copyright (c) 2007 John Wiley & Sons, Ltd.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 11