Microspectroscopic evidence of cretaceous bone proteins.

Low concentrations of the structural protein collagen have recently been reported in dinosaur fossils based primarily on mass spectrometric analyses of whole bone extracts. However, direct spectroscopic characterization of isolated fibrous bone tissues, a crucial test of hypotheses of biomolecular p...

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Autores principales:	Johan Lindgren, Per Uvdal, Anders Engdahl, Andrew H Lee, Carl Alwmark, Karl-Erik Bergquist, Einar Nilsson, Peter Ekström, Magnus Rasmussen, Desirée A Douglas, Michael J Polcyn, Louis L Jacobs
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/601a19b4678547648efeaf764ebf6f44
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spelling	oai:doaj.org-article:601a19b4678547648efeaf764ebf6f442021-11-18T06:54:51ZMicrospectroscopic evidence of cretaceous bone proteins.1932-620310.1371/journal.pone.0019445https://doaj.org/article/601a19b4678547648efeaf764ebf6f442011-04-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21559386/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Low concentrations of the structural protein collagen have recently been reported in dinosaur fossils based primarily on mass spectrometric analyses of whole bone extracts. However, direct spectroscopic characterization of isolated fibrous bone tissues, a crucial test of hypotheses of biomolecular preservation over deep time, has not been performed. Here, we demonstrate that endogenous proteinaceous molecules are retained in a humerus from a Late Cretaceous mosasaur (an extinct giant marine lizard). In situ immunofluorescence of demineralized bone extracts shows reactivity to antibodies raised against type I collagen, and amino acid analyses of soluble proteins extracted from the bone exhibit a composition indicative of structural proteins or their breakdown products. These data are corroborated by synchrotron radiation-based infrared microspectroscopic studies demonstrating that amino acid containing matter is located in bone matrix fibrils that express imprints of the characteristic 67 nm D-periodicity typical of collagen. Moreover, the fibrils differ significantly in spectral signature from those of potential modern bacterial contaminants, such as biofilms and collagen-like proteins. Thus, the preservation of primary soft tissues and biomolecules is not limited to large-sized bones buried in fluvial sandstone environments, but also occurs in relatively small-sized skeletal elements deposited in marine sediments.Johan LindgrenPer UvdalAnders EngdahlAndrew H LeeCarl AlwmarkKarl-Erik BergquistEinar NilssonPeter EkströmMagnus RasmussenDesirée A DouglasMichael J PolcynLouis L JacobsPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 4, p e19445 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Johan Lindgren Per Uvdal Anders Engdahl Andrew H Lee Carl Alwmark Karl-Erik Bergquist Einar Nilsson Peter Ekström Magnus Rasmussen Desirée A Douglas Michael J Polcyn Louis L Jacobs Microspectroscopic evidence of cretaceous bone proteins.
description	Low concentrations of the structural protein collagen have recently been reported in dinosaur fossils based primarily on mass spectrometric analyses of whole bone extracts. However, direct spectroscopic characterization of isolated fibrous bone tissues, a crucial test of hypotheses of biomolecular preservation over deep time, has not been performed. Here, we demonstrate that endogenous proteinaceous molecules are retained in a humerus from a Late Cretaceous mosasaur (an extinct giant marine lizard). In situ immunofluorescence of demineralized bone extracts shows reactivity to antibodies raised against type I collagen, and amino acid analyses of soluble proteins extracted from the bone exhibit a composition indicative of structural proteins or their breakdown products. These data are corroborated by synchrotron radiation-based infrared microspectroscopic studies demonstrating that amino acid containing matter is located in bone matrix fibrils that express imprints of the characteristic 67 nm D-periodicity typical of collagen. Moreover, the fibrils differ significantly in spectral signature from those of potential modern bacterial contaminants, such as biofilms and collagen-like proteins. Thus, the preservation of primary soft tissues and biomolecules is not limited to large-sized bones buried in fluvial sandstone environments, but also occurs in relatively small-sized skeletal elements deposited in marine sediments.
format	article
author	Johan Lindgren Per Uvdal Anders Engdahl Andrew H Lee Carl Alwmark Karl-Erik Bergquist Einar Nilsson Peter Ekström Magnus Rasmussen Desirée A Douglas Michael J Polcyn Louis L Jacobs
author_facet	Johan Lindgren Per Uvdal Anders Engdahl Andrew H Lee Carl Alwmark Karl-Erik Bergquist Einar Nilsson Peter Ekström Magnus Rasmussen Desirée A Douglas Michael J Polcyn Louis L Jacobs
author_sort	Johan Lindgren
title	Microspectroscopic evidence of cretaceous bone proteins.
title_short	Microspectroscopic evidence of cretaceous bone proteins.
title_full	Microspectroscopic evidence of cretaceous bone proteins.
title_fullStr	Microspectroscopic evidence of cretaceous bone proteins.
title_full_unstemmed	Microspectroscopic evidence of cretaceous bone proteins.
title_sort	microspectroscopic evidence of cretaceous bone proteins.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/601a19b4678547648efeaf764ebf6f44
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Microspectroscopic evidence of cretaceous bone proteins.

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