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Collagen and keratin polypeptide models for assessing the natural and artificial protein decay of organic materials
Author(s) -
Fotou Evmorfia,
SakarellosDaitsiotis Maria,
Ioakeimoglou Eleni,
Tziamourani Eleni,
Malea Ekaterini,
Panayiaris George,
PanouPomonis Eugenia
Publication year - 2016
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2933
Subject(s) - keratin , chemistry , peptide , polypeptide chain , biochemistry , amino acid , biophysics , biology , genetics
Among the materials constituting the natural and cultural heritage, organic materials of proteinaceous origin as bone (collagen), parchment and woolen textiles (keratin) are the most susceptible to damage and decay because of their exposure to air pollution, inappropriate values of ambient temperature, humidity and light. Aiming at contributing to the development of a reliable and reproducible immunoassay for the evaluation of collagen and keratin decay, three polypeptide models of these proteins were designed, synthesized and studied. Polypeptide [Pro‐Ser(OBzl)‐Gly] n incorporates the typical motif Pro‐X‐Gly of collagen; polypeptide [Pro‐Cys(Acm)‐Gly] n is a model of the C‐terminal domain of type I keratin, corresponding to the repeating unit Pro‐Cys‐X of keratin, while polypeptide Ac‐YRSGGGFGYRSGGGFGYRS‐βAla‐NH 2 encloses the characteristic repeating sequence GGGFGYRS of the N‐terminal part of Type II keratin. These polypeptides may be considered as simplified models that mimic fragments of collagen and keratin resulting from artificial and natural ageing or decay. It is concluded that high recognition of anti‐polypeptide antibodies, produced after immunizations, by the bone, parchment and textile samples is indicative of high deterioration, while high anti‐collagen or anti‐keratin recognition is indicative of low deterioration. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.