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Calcified Tissue International

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28.02.2017 | Original Research

Identification of Pyridinoline Trivalent Collagen Cross-Links by Raman Microspectroscopy

verfasst von: Sonja Gamsjaeger, Simon P. Robins, Dimitris N. Tatakis, Klaus Klaushofer, Eleftherios P. Paschalis

Erschienen in: Calcified Tissue International | Ausgabe 6/2017

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Abstract

Intermolecular cross-linking of bone collagen is intimately related to the way collagen molecules are arranged in a fibril, imparts certain mechanical properties to the fibril, and may be involved in the initiation of mineralization. Raman microspectroscopy allows the analysis of minimally processed bone blocks and provides simultaneous information on both the mineral and organic matrix (mainly type I collagen) components, with a spatial resolution of ~1 μm. The aim of the present study was to validate Raman spectroscopic parameters describing one of the major mineralizing type I trivalent cross-links, namely pyridinoline (PYD). To achieve this, a series of collagen cross-linked peptides with known PYD content (as determined by HPLC analysis), human bone, porcine skin, predentin and dentin animal model tissues were analyzed by Raman microspectroscopy. The results of the present study confirm that it is feasible to monitor PYD trivalent collagen cross-links by Raman spectroscopic analysis in mineralized tissues, exclusively through a Raman band ~1660 wavenumbers. This allows determination of the relative PYD content in undecalcified bone tissues with a spatial resolution of ~1 μm, thus enabling correlations with histologic and histomorphometric parameters.

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Titel: Identification of Pyridinoline Trivalent Collagen Cross-Links by Raman Microspectroscopy
verfasst von: Sonja Gamsjaeger
Simon P. Robins
Dimitris N. Tatakis
Klaus Klaushofer
Eleftherios P. Paschalis
Publikationsdatum: 28.02.2017
Verlag: Springer US
Erschienen in: Calcified Tissue International / Ausgabe 6/2017
Print ISSN: 0171-967X
Elektronische ISSN: 1432-0827
DOI: https://doi.org/10.1007/s00223-016-0232-5

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