gms | German Medical Science

54. Jahrestagung der Norddeutschen Orthopädenvereinigung e. V.

Norddeutsche Orthopädenvereinigung

16.06. bis 18.06.2005, Hamburg

Solid-state NMR spectroscopy on bone: first results and perspectives

Meeting Abstract

  • corresponding author M. Pretzsch - Orthopädische Klinik und Poliklinik am Universitätsklinikum AöR, Leipzig
  • A. Wild - Leipzig
  • J. Schulz - Leipzig
  • G. Zernia - Leipzig
  • A. Deiwick - Leipzig
  • A. Bader - Leipzig
  • K. Arnold - Leipzig
  • D. Huster - Leipzig

Norddeutsche Orthopädenvereinigung. 54. Jahrestagung der Norddeutschen Orthopädenvereinigung e.V.. Hamburg, 16.-18.06.2005. Düsseldorf, Köln: German Medical Science; 2005. Doc05novEP29

The electronic version of this article is the complete one and can be found online at:

Published: June 13, 2005

© 2005 Pretzsch et al.
This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( You are free: to Share – to copy, distribute and transmit the work, provided the original author and source are credited.



We have investigated rabbit bone samples by 31P and 13C solid state NMR spectroscopy in order to understand the molecular organization of the major organic and inorganic molecular components of bone, collagen type I and calcium-hydroxyapatite. High resolution of the solid-state NMR spectra is obtained by magic angle spinning. The 31P spectra of bone specimen show a single line characteristic for calcium-hydroxyapatite. 13C CPMAS NMR spectra show the characteristic signatures of collagen type I with good resolution for all major amino acids in collagen (alanine, glycine, proline, and hydroxyproline). Quantitative measurements of 13C-1H dipolar couplings indicate that the collagen segments are very rigid with only small amplitude motions with correlation times in the nanosecond range. These quantitative investigations of natural bone may provide the basis for a quality control of all osteoinductive bone substitutes. If the artificial material is well adapted into the bone, collagen type I and calcium-hydroxyapatite should be detectable by the NMR technique. To test this idea, an animal study is currently carried out. From the 31P NMR spectra, ß-tricalcium phosphate and calcium-hydroxyapatite can be distinguished quantitatively. This should allow to record the formation of natural bone material. Further, 13C CPMAS spectra should allow to detect collagen type I that has been produced from the cells. Comparison with the spectroscopic date from natural bone should allow to assess the quality of the bone substitute material.