ArticleScientific reports2020
Linking structural and compositional changes in archaeological human bone collagen: an FTIR-ATR approach.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 70 citations in OpenAlex.
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- A fresh perspective on infrared spectroscopy as a prescreening method for molecular and stable isotopes analyses on ancient human bones.Scientific reports · 2024Article
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- Comparison of DNA preservation and ATR-FTIR spectroscopy indices of cortical and trabecular bone of metacarpals and metatarsals.Scientific reports · 2023Article
- Molecular Quantity Variations in Human-Mandibular-Bone Osteoid.Calcified tissue international · 2022Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collagen is the main structural and most abundant protein in the human body, and it is routinely extracted and analysed in scientific archaeology. Its degree of preservation is, therefore, crucial and several approaches are used to determine it. Spectroscopic techniques provide a cost-effective, non-destructive method to investigate the molecular structure, especially when combined with multivariate statistics (chemometric approach). In this study, we used FTIR-ATR spectroscopy to characterise collagen extracted from skeletons recovered from necropoleis in NW Spain spanning from the Bronze Age to eighteenth century AD. Principal components analysis was performed on a selection of bands and structural equation models (SEM) were developed to relate the collagen quality indicators to collagen structural change. Four principal components represented: (i) Cp1, transformations of the backbone protein with a residual increase in proteoglycans; (ii) Cp2, protein transformations not accompanied by changes in proteoglycans abundance; (iii) Cp3, variations in aliphatic side chains and (iv) Cp4, absorption of the OH of carbohydrates and amide. Highly explanatory SEM models were obtained for the traditional collagen quality indicators (collagen yield, C, N, C:N), but no relationship was found between quality and δ
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