Effect of Structural Modification on Second Harmonic Generation in Collagen
The effects of structural perturbation on second harmonic generation in collagen were investigated. Type I collagen fascicles obtained from rat tails were structurally modified by increasing nonenzymatic cross-linking, by thermal denaturation, by collagenase digestion, or by dehydration. Changes in polarization dependence were observed in the dehydrated samples. Surprisingly, no changes in polarization dependence were observed in highly crosslinked samples, despite significant alterations in packing structure. Complete thermal denaturation and collagenase digestion produced samples with no detectable second harmonic signal. Prior to loss of signal, no change in polarization dependence was observed in partially heated or digested collagen.
- Research Organization:
- Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
- Sponsoring Organization:
- US Department of Energy (US)
- DOE Contract Number:
- W-7405-ENG-48
- OSTI ID:
- 15005077
- Report Number(s):
- UCRL-JC-152693; TRN: US200414%%575
- Resource Relation:
- Journal Volume: 4963; Conference: SPIE Conference on Visualization and Data Analysis, San Jose, CA (US), 01/20/2003--01/25/2003; Other Information: PBD: 4 Apr 2003
- Country of Publication:
- United States
- Language:
- English
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