ProArc · The protein archive: preservation potential of ancient human diets and diseases.

The protein archive: preservation potential of ancient human diets and diseases.

Milk proteins are widely reported in the archaeological record, and are dominated by two classes, both widely studied in the food industry: acid-insoluble caseins (the main component of curds) and acid-soluble lactoglobulins (whey proteins). Dental calculus is regarded by many as the most informative ancient remains and is in high demand, being used to explore: ancient diets and human-environment interaction. One surprising find is that whey protein (β-lactoglobulin; BLG) is typically the only protein preserved in ancient dental calculus (apatite?), whereas lime-scale (calcite) from ceramics shows the survival of both the milk proteins curd (caseins) and whey (lactoglobulins). For both the calculus and the ceramic scale, the proteins are extracted in a similar manner, and their burial environment is not distinct enough to play a role for the different survival. The paucity of milk proteins on calculus contrasted with their comparative abundance on ceramics implies selective differences in incorporation or preservation. Understanding the protein-mineral interaction is key both for accessing the mechanisms controlling the protein-mineral interactions and understanding the longevity of minerals preserved different (milk) protein record in deep time. Therefore, ProArc aims to address 4 research objectives (RO): RO1: assess different ancient protein-mineral associations and preservation states in potsherds from different archaeological sites to map the differences in physical and chemical storage conditions over time. RO2: investigate the in vitro organic-molecules-mineral interactions of mineral at the single bond level (bond breaking and reforming) in different relevant solution compositions to quantify the energy and kinetic parameters associated with the interacting bonds. RO3. examine the organic-mineral interactions at the bulk level (nature, fraction and stability of interacting bonds) and link those to the single bond level energetics to quantify the longevity of the biomolecule-mineral in different environmentally relevant solution compositions. RO4. link the archaeological biomolecules data to the in vitro single bond and bulk data then make a conceptual model for addressing the characteristics and longevity of biomolecule-mineral system(s), and improve our understanding of cultural heritage of milk protein. Overall, our Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analyses of archeological remains, AFM (nano-imaging, rupture forces), FTIR data, and ultraviolet data (adsorption isotherms) suggest that the milk protein-mineral association is strongly influenced by the interfacial geochemistry and it is sensitive to mineral surface charge, mineral charge density, pH, solution composition and solution salinity.

Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз