caa a22 4500 605521093 CHVBK 20210128100738.0 cr unu---uuuuu 210128e20150101xx s 000 0 eng 10.1007/s00223-014-9933-9 doi (NATIONALLICENCE)springer-10.1007/s00223-014-9933-9 Fourier Transform Infrared Spectroscopic Characterization of Mineralizing Type I Collagen Enzymatic Trivalent Cross-Links [Elektronische Daten] [E. Paschalis, S. Gamsjaeger, D. Tatakis, N. Hassler, S. Robins, K. Klaushofer] The most abundant protein of bone's organic matrix is collagen. One of its most important properties is its cross-linking pattern, which is responsible for the fibrillar matrices' mechanical properties such as tensile strength and viscoelasticity. We have previously described a spectroscopic method based on the resolution of the Amide I and II Fourier transform Infrared (FTIR) bands to their underlying constituent peaks, which allows the determination of divalent and pyridinoline (PYD) collagen cross-links in mineralized thin bone tissue sections with a spatial resolution of ~6.3μm. In the present study, we used FTIR analysis of a series of biochemically characterized collagen peptides, as well as skin, dentin, and predentin, to examine the potential reasons underlying discrepancies between two different analytical methodologies specifically related to spectral processing. The results identified a novel distinct FTIR underlying peak at ~1,680cm−1, correlated with deoxypyridinoline (DPD) content. Furthermore, the two different methods of spectral resolution result in widely different results, while only the method employing well-established spectroscopic routines for spectral resolution provided biologically relevant results, confirming our earlier studies relating the area of the underlying 1,660cm−1 with PYD content. The results of the present study describe a new peak that may be used to determine DPD content, confirm our earlier report relating spectroscopic parameters to PYD content, and highlight the importance of the selected spectral resolution methodology. Springer Science+Business Media New York, 2014 Collagen cross-links nationallicence Fourier transform infrared spectroscopy nationallicence Second derivative spectroscopy nationallicence Pyridinoline nationallicence Deoxypyridinoline nationallicence Paschalis E. Ludwig Boltzmann Institute of Osteology at the Hanusch Hospital of WGKK and AUVA Trauma Centre Meidling, 1st Medical Department, Hanusch Hospital, Hanusch Krankenhaus, Heinrich Collin Str. 30, 1140, Vienna, Austria aut Gamsjaeger S. Ludwig Boltzmann Institute of Osteology at the Hanusch Hospital of WGKK and AUVA Trauma Centre Meidling, 1st Medical Department, Hanusch Hospital, Hanusch Krankenhaus, Heinrich Collin Str. 30, 1140, Vienna, Austria aut Tatakis D. Division of Periodontology, College of Dentistry, The Ohio State University, Columbus, OH, USA aut Hassler N. Ludwig Boltzmann Institute of Osteology at the Hanusch Hospital of WGKK and AUVA Trauma Centre Meidling, 1st Medical Department, Hanusch Hospital, Hanusch Krankenhaus, Heinrich Collin Str. 30, 1140, Vienna, Austria aut Robins S. Matrix Biochemistry, Rowett Institute of Nutrition and Health, University of Aberdeen, Bucksburn, AB21 9SB, Aberdeen, UK aut Klaushofer K. Ludwig Boltzmann Institute of Osteology at the Hanusch Hospital of WGKK and AUVA Trauma Centre Meidling, 1st Medical Department, Hanusch Hospital, Hanusch Krankenhaus, Heinrich Collin Str. 30, 1140, Vienna, Austria aut Calcified Tissue International Springer US; http://www.springer-ny.com 96/1(2015-01-01), 18-29 0171-967X 96:1<18 2015 96 223 https://doi.org/10.1007/s00223-014-9933-9 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00223-014-9933-9 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Paschalis E. Ludwig Boltzmann Institute of Osteology at the Hanusch Hospital of WGKK and AUVA Trauma Centre Meidling, 1st Medical Department, Hanusch Hospital, Hanusch Krankenhaus, Heinrich Collin Str. 30, 1140, Vienna, Austria aut NATIONALLICENCE 700 1- Gamsjaeger S. Ludwig Boltzmann Institute of Osteology at the Hanusch Hospital of WGKK and AUVA Trauma Centre Meidling, 1st Medical Department, Hanusch Hospital, Hanusch Krankenhaus, Heinrich Collin Str. 30, 1140, Vienna, Austria aut NATIONALLICENCE 700 1- Tatakis D. Division of Periodontology, College of Dentistry, The Ohio State University, Columbus, OH, USA aut NATIONALLICENCE 700 1- Hassler N. Ludwig Boltzmann Institute of Osteology at the Hanusch Hospital of WGKK and AUVA Trauma Centre Meidling, 1st Medical Department, Hanusch Hospital, Hanusch Krankenhaus, Heinrich Collin Str. 30, 1140, Vienna, Austria aut NATIONALLICENCE 700 1- Robins S. Matrix Biochemistry, Rowett Institute of Nutrition and Health, University of Aberdeen, Bucksburn, AB21 9SB, Aberdeen, UK aut NATIONALLICENCE 700 1- Klaushofer K. Ludwig Boltzmann Institute of Osteology at the Hanusch Hospital of WGKK and AUVA Trauma Centre Meidling, 1st Medical Department, Hanusch Hospital, Hanusch Krankenhaus, Heinrich Collin Str. 30, 1140, Vienna, Austria aut NATIONALLICENCE 773 0- Calcified Tissue International Springer US; http://www.springer-ny.com 96/1(2015-01-01), 18-29 0171-967X 96:1<18 2015 96 223