Effect of structural modification on second harmonic generation in collagen | Zendy

Patrick Stoller | Zendy; Karen M. Reiser | Zendy; P. M. Celliers | Zendy; Alexander M. Rubenchik | Zendy

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Effect of structural modification on second harmonic generation in collagen

Author(s) -

Patrick Stoller,

Karen M. Reiser,

P. M. Celliers,

Alexander M. Rubenchik

Publication year - 2003

Publication title -

proceedings of spie, the international society for optical engineering/proceedings of spie

Language(s) - English

Resource type - Conference proceedings

SCImago Journal Rank - 0.192

H-Index - 176

eISSN - 1996-756X

pISSN - 0277-786X

DOI - 10.1117/12.477998

Subject(s) - collagenase , denaturation (fissile materials) , chemistry , polarization (electrochemistry) , biophysics , type i collagen , dehydration , materials science , crystallography , enzyme , biochemistry , nuclear chemistry , biology , medicine , pathology

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.

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