Chemical evidence of preserved collagen in a 54-million-year-old fish vertebrae
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Dec 18, 2019 version files 5.09 MB
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Abstract
Collagens are the most abundant protein in the animal kingdom. Collagens form the structural framework of connective tissues such as bones, tendons and skin and play important biomechanical role in supporting tissue functions. The preservation of collagen in deep time is a topic of intense debate. Here we provide indisputable evidence of the presence of collagen in Early Eocene fish vertebrae using online pyrolysis-comprehensive two dimensional gas chromatography-time-of-flight mass spectrometry and immunofluorescence studies. The presence of cyclic dipeptides such as diketodipyrrole, 2,5-diketopiperazine of proline-proline and 2,5-diketopiperazine of proline-glycine along with other nitrogen-bearing molecules in the pyrolysis products of the studied fossils unequivocally demonstrate that collagen can withstand degradation and diagenetic alteration. Immunofluorescence study also confirms the presence of collagen-I in the fossilized fish vertebrae. The present findings suggest, contrary to common opinion, that the preservation of collagen in fossilized soft tissues is not rare. We propose that one of the essential factors controlling preservation of collagen is the establishment of a suitable microenvironment within the fossil inhibiting diagenetic alteration including microbial decay.
Usage notes
Supplemental material for the associated article in Palaeontology.