Please use this identifier to cite or link to this item: https://hdl.handle.net/10216/91720
Author(s): vitorino, r
calheiros-lobo, mj
williams, j
ferrer-correia, aj
tomer, kb
duarte, ja
domingues, pm
amado, fm
Title: Peptidomic analysis of human acquired enamel pellicle
Issue Date: 2007
Abstract: 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.
Subject: Ciências biológicas
Biological sciences
Scientific areas: Ciências exactas e naturais::Ciências biológicas
Natural sciences::Biological sciences
URI: https://hdl.handle.net/10216/91720
Document Type: Artigo em Revista Científica Internacional
Rights: restrictedAccess
Appears in Collections:FADEUP - Artigo em Revista Científica Internacional

Files in This Item:
File Description SizeFormat 
45157.pdf
  Restricted Access
1.02 MBAdobe PDF    Request a copy from the Author(s)


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.