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 |
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Authors: | Angela Chambery Antimo Di Maro Carmen Sanges Valeria Severino Maura Tarantino Annalisa Lamberti Augusto Parente Paolo Arcari |
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Institution: | 1.Dipartimento di Scienze della Vita,Seconda Università di Napoli,Caserta,Italy;2.Dipartimento di Biochimica e Biotecnologie Mediche,Università di Napoli Federico II,Naples,Italy;3.CEINGE Biotecnologie Avanzate Scarl,Naples,Italy |
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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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