Proteomics

Dataset Information

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Enhancing ZooMS applications with MALDI-FTICR mass spectrometry on Pleistocene material showing variable collagen preservation


ABSTRACT: Advances in high-throughput molecular analyses of collagen peptides, especially ZooMS (Zooarchaeology by Mass Spectrometry), have addressed the issue of intense skeletal fragmentation at Palaeolithic archaeological sites, which hinders morphological identification. However, the challenge of variable collagen preservation persists. We aim to evaluate the potential of two mass analyzers TOF vs FTICR to propose novel options to enhance the ZooMS workflow. Type 1 collagen (COL1) was extracted from 89 archaeological bones from the site of Le Piage (France, 37-34 ka cal BP). Three distinct ZooMS protocols were used: an acid-free method (AmBic) and two demineralizations (HCl and TFA), combined with MALDI-TOF and MALDI-FTICR instruments. The first offers rapid and cheap analysis, while the second provides higher resolution. Taxonomic identifications were made by peptide mass fingerprinting (PMF). Finally, LC-MS/MS was applied to verify 26 low-collagen samples identifications.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Bos Taurus (bovine) Rangifer Tarandus (reindeer) (cervus Tarandus)

TISSUE(S): Bone

SUBMITTER: BRAY FABRICE  

LAB HEAD: fabrice bray

PROVIDER: PXD056898 | Pride | 2025-03-17

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
100424-PRM-Pauline.zip Other
LePiage-PD-homemade.zip Other
LePiage-PD-uniprot.zip Other
Lepiage-DDA.zip Other
MALDI-CASI-FTICR.zip Other
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Publications

Using MALDI-FTICR Mass Spectrometry to Enhance ZooMS Identifications of Pleistocene Bone Fragments Showing Variable Collagen Preservation.

Raymond Pauline P   Ruebens Karen K   Bray Fabrice F   Castel Jean-Christophe JC   Morin Eugène E   Le Brun-Ricalens Foni F   Bordes Jean-Guillaume JG   Rolando Christian C   Hublin Jean-Jacques JJ  

Rapid communications in mass spectrometry : RCM 20250308


<h4>Rationale</h4>Recent advances in high-throughput molecular analyses of collagen peptides, especially ZooMS (Zooarchaeology by Mass Spectrometry), have permitted breakthroughs in the analysis of archaeological material that is highly fragmented, a factor that hinders morphological identification. Despite these advances, the challenge of successfully analysing archaeological samples with poorer collagen preservation persists. This paper examines the potential of two mass analysers, TOF (Time o  ...[more]

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