Synchrotron Chemical and Structural Analysis of Tyrannosaurus rex Blood Vessels: The Contribution of Collagen Hypercrosslinking to Tissue Longevity

Recent descriptions of blood vessels recovered from dinosaur bones have raised many questions regarding tissue diagenesis and the associated chemical pathways that led to preservation. Previous analyses have identified preserved elastin and collagen proteins in a variety of specimens [1][2]. In particular, the mechanical, chemical, and thermal susceptibility of fibrillar collagen is partially dependent on the degree of intermolecular crosslinking. While collagen crosslinking can be either enzymatically or non-enzymatically driven in life, in death, only non-enzymatic pathways are available. Hence, non-enzymatic intermolecular crosslinking of fibrillar collagen supermolecular networks in fossil blood vessels has been suggested as a possible contributor to tissue longevity.