Fourier Transform Infrared Spectroscopic Characterization of Mineralizing Type I Collagen Enzymatic Trivalent Cross-Links

Verfasser / Beitragende:
[E. Paschalis, S. Gamsjaeger, D. Tatakis, N. Hassler, S. Robins, K. Klaushofer]
Ort, Verlag, Jahr:
2015
Enthalten in:
Calcified Tissue International, 96/1(2015-01-01), 18-29
Format:
Artikel (online)
ID: 605521093
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024 7 0 |a 10.1007/s00223-014-9933-9  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00223-014-9933-9 
245 0 0 |a Fourier Transform Infrared Spectroscopic Characterization of Mineralizing Type I Collagen Enzymatic Trivalent Cross-Links  |h [Elektronische Daten]  |c [E. Paschalis, S. Gamsjaeger, D. Tatakis, N. Hassler, S. Robins, K. Klaushofer] 
520 3 |a 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. 
540 |a Springer Science+Business Media New York, 2014 
690 7 |a Collagen cross-links  |2 nationallicence 
690 7 |a Fourier transform infrared spectroscopy  |2 nationallicence 
690 7 |a Second derivative spectroscopy  |2 nationallicence 
690 7 |a Pyridinoline  |2 nationallicence 
690 7 |a Deoxypyridinoline  |2 nationallicence 
700 1 |a Paschalis  |D E.  |u 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  |4 aut 
700 1 |a Gamsjaeger  |D S.  |u 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  |4 aut 
700 1 |a Tatakis  |D D.  |u Division of Periodontology, College of Dentistry, The Ohio State University, Columbus, OH, USA  |4 aut 
700 1 |a Hassler  |D N.  |u 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  |4 aut 
700 1 |a Robins  |D S.  |u Matrix Biochemistry, Rowett Institute of Nutrition and Health, University of Aberdeen, Bucksburn, AB21 9SB, Aberdeen, UK  |4 aut 
700 1 |a Klaushofer  |D K.  |u 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  |4 aut 
773 0 |t Calcified Tissue International  |d Springer US; http://www.springer-ny.com  |g 96/1(2015-01-01), 18-29  |x 0171-967X  |q 96:1<18  |1 2015  |2 96  |o 223 
856 4 0 |u https://doi.org/10.1007/s00223-014-9933-9  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
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950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00223-014-9933-9  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Paschalis  |D E.  |u 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  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Gamsjaeger  |D S.  |u 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  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Tatakis  |D D.  |u Division of Periodontology, College of Dentistry, The Ohio State University, Columbus, OH, USA  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Hassler  |D N.  |u 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  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Robins  |D S.  |u Matrix Biochemistry, Rowett Institute of Nutrition and Health, University of Aberdeen, Bucksburn, AB21 9SB, Aberdeen, UK  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Klaushofer  |D K.  |u 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  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Calcified Tissue International  |d Springer US; http://www.springer-ny.com  |g 96/1(2015-01-01), 18-29  |x 0171-967X  |q 96:1<18  |1 2015  |2 96  |o 223