Résumé
Collagen is the main organic component preserved in archaeological bones and represents a key molecular archivefor reconstructing past societies. Over the last decade, mass spectrometry has become central to archaeologicalbiomolecular research, notably through the development of Zooarchaeology by Mass Spectrometry (ZooMS) whichenables taxonomic identification of highly fragmented remains [1]. Beyond species identification, collagen peptideprofiles can also provide information on molecular degradation and post translational modifications (PTMs), openingnew perspectives on diagenetic processes [2].This project aims to develop a Matrix-Assisted Laser Desorption/Ionization-Time of Flight (MALDI-ToF) massspectrometry-based screening workflow to evaluate collagen preservation in faunal remains from late prehistoricMediterranean contexts. Samples will originate from seven archaeological sites covering a diverse set of depositionalenvironments. Collagen will be extracted using established demineralisation and gelatinisation protocols. Peptidemass fingerprints will be acquired by MALDI-ToF mass spectrometry in positive mode (RAPIFLEX, Bruker) followingenzymatic digestion. Collagen preservation will be assessed using qualitative and semi quantitative indicators such asdiagnostic peptide abundance and detection of degradation related modifications [3]. Comparative analysis betweensites will be conducted to investigate the influence of environmental parameters and burial conditions.The expected outcomes include the establishment of a robust screening protocol for rapid evaluation of collagenintegrity using MALDI-ToF mass spectrometry. The study aims to identify preservation trends across Mediterraneanarchaeological contexts and to formulate hypotheses regarding environmental drivers of molecular degradation. Thisapproach will allow optimisation of sampling strategies for subsequent high resolution proteomic and isotopicinvestigations. Ultimately, this work will contribute to methodological standardisation in archaeological proteomicsand improve the efficiency of biomolecular studies on non-homogeneously preserved remains.