Effect of structural modification on second harmonic generation in collagen

Patrick Christian Stoller; Karen M. Reiser; Peter M. Celliers; Alexander M. Rubenchik

doi:10.1117/12.477998

10 July 2003 Effect of structural modification on second harmonic generation in collagen

Patrick Christian Stoller, Karen M. Reiser, Peter M. Celliers, Alexander M. Rubenchik

Proceedings Volume 4963, Multiphoton Microscopy in the Biomedical Sciences III; (2003) https://doi.org/10.1117/12.477998
Event: Biomedical Optics, 2003, San Jose, CA, United States

Abstract

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.

Citation Download Citation

Patrick Christian Stoller, Karen M. Reiser, Peter M. Celliers, and Alexander M. Rubenchik "Effect of structural modification on second harmonic generation in collagen", Proc. SPIE 4963, Multiphoton Microscopy in the Biomedical Sciences III, (10 July 2003); https://doi.org/10.1117/12.477998

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