Abstract
Proteinaceous substances such as collagen, casein and albumin have been widely used as binding media in a variety of works of art. Damages of these ‘sensitive’ materials, mainly caused of the influence of the environment, are responsible for the overall decay of works of art, and their identification is essential to understand ancient technologies, determine the extent of deterioration and help in future restoration and preservation processes. The most commonly used techniques for the identification of proteinaceous binding media are staining techniques, chromatography, spectrometry and immunological methods, although for the latter no systematic studies have been carried out until now. Aiming at contributing to the development of a reliable and reproducible immunoassay for the evaluation of the collagen‐based decay of works of art, sequential polypeptides (Pro‐X‐Gly)~n~ where X represents amino acid residues Val, Lys, Glu and (Hyp‐Val‐Gly)~n~ were prepared as models of collagen fragments derived from artificially and naturally aged animal collagens. Conformational studies of the polypeptides by CD revealed the occurrence of polyproline II‐like structures comparable with those of collagen. Polypeptides and collagen I were administered to animals, and the induced antibodies were used for the immunochemical detection and differentiation of collagen and collagen fragments. The combined application of (i) anti‐collagen antibodies, which strongly interact with native collagen, but poorly recognized by artificially aged collagen and (ii) anti‐polypeptide antibodies, which do not associate with native collagen, but are strongly recognized by collagen fragments in naturally or artificially aged collagen, is a valuable tool in determining the extent of decay in works of art. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.