The Mummy: Cangrande della Scala in Life and Protein Science

by | May 27, 2017

Researchers report a study on the proteins of the natural mummy of Cangrande della Scala (Prince of Verona, Northern Italy).

In this Protein Science paper, Ivan Mikšík from the Institute of Physiology of the Czech Academy of Sciences and colleagues from the University of Verona report a study on the proteins of the natural mummy of Cangrande della Scala (Prince of Verona, Northern Italy).

A nobleman, a successful warrior, and autocrat, Cangrande was a notable historical figure of his times. He was also the leading patron of the Italian poet Dante Alighieri. Born in Verona in 1291, Cangrande’s reign lasted from 1311 to his death in Treviso on July 22, 1329. He was buried with great fanfare in a marble tomb in the church of Santa Maria Antiqua of Verona.

In 2004, Cangrande’s body was exhumed for an archaeo-pathological forensic investigation of his death. Instead of skeletal or poorly preserved remains, the scientists found a well-preserved mummy. Most likely due to a quick drying environment of the stone sarcophagus he was buried in. The forensic analysis confirmed a foul play: Cangrande was poisoned by lethal doses of the drug digitalis, masquerading as the medical treatment for water-borne infection. Who murdered him and why? Still a mystery! But that’s another story that might never be told.

The nano-LC-Q-TOF, or nano-Liquid Chromatography-Quadrupole Time of Flight method of mass spectrometry analysis of Cangrande’s rib bone and muscle revealed different proteins including Types I, III, IV, V, and XI collagen, hemoglobin (subunits alpha and beta), ferritin, biglycan, vitronectin, prothrombin, and osteocalcin. Mikšík and colleagues studied the structure of type I and type III collagen in more detail. The analysis showed a high percentage of asparaginyl and glutaminyl deamidation, carbamylation and carboxymethylation of lysine. The most common reaction during the natural mummification process was oxidation – hydroxylation of lysine andproline as well as oxidation (and dioxidation) of methionine.

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