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Proteins and their modifications in a medieval mummy
Ivan Mikšík1, Pavla Sedláková2, Statis Pataridis2
1Institute of Physiology, Academy of Sciences of the Czech Republic, Prague, 14220, Czech Republic. ivan.miksik@fgu.cas.cz.
Protein Science : a Publication of the Protein Society
|August 21, 2016
Summary
This study analyzed proteins in the mummy of Cangrande della Scala, revealing significant modifications like oxidation and deamidation in collagen and other proteins during natural mummification.
Area of Science:
- Biochemistry
- Proteomics
- Paleopathology
Background:
- Investigating the molecular preservation of ancient human remains offers insights into decomposition processes.
- Natural mummification preserves tissues, allowing for detailed biochemical analysis.
Observation:
- Proteomic analysis of Cangrande della Scala's mummy (rib bone and muscle) identified key proteins: collagens (Types I, III, IV, V, XI), hemoglobin, ferritin, biglycan, vitronectin, prothrombin, and osteocalcin.
- Detailed structural examination of Type I and Type III collagen revealed extensive post-translational modifications.
Findings:
- High levels of asparaginyl and glutaminyl deamidation were observed.
- Carbamylation and carboxymethylation of lysine residues were identified.
- Oxidation and dioxidation of methionine were prevalent, alongside hydroxylation of lysine and proline in collagen Type I.
Implications:
- This research provides the first protein profile of naturally mummified human tissue.
- It is the first study to document carbamylation and carboxymethylation of lysine in mummified samples.
- Understanding these protein modifications enhances our knowledge of diagenesis and biomolecular preservation in ancient tissues.
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