Abstract
Diagnostic techniques applied to the field of cultural heritage represent a very important aspect of scientific investigation. Recently, proteomic approaches based on mass spectrometry coupled with traditional spectroscopic methods have been used for painting analysis, generating promising results for binder’s protein identification. In the present work, an improved procedure based on LC-ESI/Q-q-TOF tandem mass spectrometry for the identification of protein binders has been developed for the molecular characterization of samples from an early-twentieth-century mural painting from the St. Dimitar Cathedral in Vidin, Bulgaria. The proteomic investigation has led to the identification of both egg white and egg yolk proteins, according to traditional old recipes for tempera paintings. In addition, beyond the egg components, the presence of caseins was also revealed, thus suggesting the use of milk as binding medium, fixative or stabilising agent. Furthermore, for the first time, the capability to discriminate the milk origin on the basis of alpha casein proteotypic peptides is reported, that are diagnostic for a given species, thus opening interesting perspectives in art and archaeological fields.
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Acknowledgements
We gratefully acknowledge Prof. Ciro Piccioli of Academy of Fine Arts of Naples for his useful encouragements and support and Dr. Ruvo Menotti of Istituto di Biostrutture e Bioimmagini, CNR of Napoli for carefully reading the manuscript. We are also grateful to Dr. Filomena Schiano Lomoriello from the “Suor Orsola Benincasa” University (Naples) for useful suggestions. This study was supported by funds from the Second University of Naples.
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Angela Chambery and Antimo Di Maro contributed equally to this work.
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Chambery, A., Di Maro, A., Sanges, C. et al. Improved procedure for protein binder analysis in mural painting by LC-ESI/Q-q-TOF mass spectrometry: detection of different milk species by casein proteotypic peptides. Anal Bioanal Chem 395, 2281–2291 (2009). https://doi.org/10.1007/s00216-009-3183-0
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DOI: https://doi.org/10.1007/s00216-009-3183-0