Spatial analysis of the ancient proteome of archeological teeth using mass spectrometry imaging.

Autor: Dekker J; BioArCh, Department of Archaeology, University of York, York, UK.; Section for GeoBiology, Globe Institute, University of Copenhagen, Copenhagen, Denmark.; Faculty of Archaeology, Leiden University, Leiden, the Netherlands., Larson T; Metabolomics & Proteomics Laboratory, Bioscience Technology Facility, Department of Biology, University of York, York, UK., Tzvetkov J; Department of Biology, University of York, York, UK., Harvey VL; BioArCh, Department of Archaeology, University of York, York, UK.; Department of Biological Sciences, University of Chester, Chester, UK., Dowle A; Metabolomics & Proteomics Laboratory, Bioscience Technology Facility, Department of Biology, University of York, York, UK., Hagan R; BioArCh, Department of Archaeology, University of York, York, UK., Genever P; Department of Biology, University of York, York, UK., Schrader S; Faculty of Archaeology, Leiden University, Leiden, the Netherlands., Soressi M; Faculty of Archaeology, Leiden University, Leiden, the Netherlands., Hendy J; BioArCh, Department of Archaeology, University of York, York, UK.
Jazyk: angličtina
Zdroj: Rapid communications in mass spectrometry : RCM [Rapid Commun Mass Spectrom] 2023 Apr 30; Vol. 37 (8), pp. e9486.
DOI: 10.1002/rcm.9486
Abstrakt: Rationale: Proteins extracted from archaeological bone and teeth are utilised for investigating the phylogeny of extinct and extant species, the biological sex and age of past individuals, as well as ancient health and physiology. However, variable preservation of proteins in archaeological materials represents a major challenge.
Methods: To better understand the spatial distribution of ancient proteins preserved within teeth, we applied matrix assisted laser desorption/ionisation mass spectrometry imaging (MALDI-MSI) for the first time to bioarchaeological samples to visualise the intensity of proteins in archaeological teeth thin sections. We specifically explored the spatial distribution of four proteins (collagen type I, of which the chains alpha-1 and alpha-2, alpha-2-HS-glycoprotein, haemoglobin subunit alpha and myosin light polypeptide 6).
Results: We successfully identified ancient proteins in archaeological teeth thin sections using mass spectrometry imaging. The data are available via ProteomeXchange with identifier PXD038114. However, we observed that peptides did not always follow our hypotheses for their spatial distribution, with distinct differences observed in the spatial distribution of several proteins, and occasionally between peptides of the same protein.
Conclusions: While it remains unclear what causes these differences in protein intensity distribution within teeth, as revealed by MALDI-MSI in this study, we have demonstrated that MALDI-MSI can be successfully applied to mineralised bioarchaeological tissues to detect ancient peptides. In future applications, this technique could be particularly fruitful not just for understanding the preservation of proteins in a range of archaeological materials, but making informed decisions on sampling strategies and the targeting of key proteins of archaeological and biological interest.
(© 2023 The Authors. Rapid Communications in Mass Spectrometry published by John Wiley & Sons Ltd.)
Databáze: MEDLINE
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