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.

[1]  Beop-Min Kim,et al.  Polarization-dependent optical second-harmonic imaging of a rat-tail tendon. , 2002, Journal of biomedical optics.

[2]  Aaas News,et al.  Book Reviews , 1893, Buffalo Medical and Surgical Journal.

[3]  Jeffrey A. Squier,et al.  High resolution nonlinear microscopy: A review of sources and methods for achieving optimal imaging , 2001 .

[4]  L M Loew,et al.  Second-harmonic imaging microscopy of living cells. , 2001, Journal of biomedical optics.

[5]  A M Rubenchik,et al.  Collagen structure and nonlinear susceptibility: Effects of heat, glycation, and enzymatic cleavage on second harmonic signal intensity , 2000, Lasers in surgery and medicine.

[6]  C. C. Wang,et al.  Nonlinear optics. , 1966, Applied optics.

[7]  Patrick Stoller,et al.  Polarization-modulated second harmonic generation in collagen. , 2002, Biophysical journal.

[8]  William A Mohler,et al.  Three-dimensional high-resolution second-harmonic generation imaging of endogenous structural proteins in biological tissues. , 2002, Biophysical journal.

[9]  R R Alfano,et al.  Second-harmonic tomography of tissues. , 1997, Optics letters.

[10]  B. Tromberg,et al.  Imaging cells and extracellular matrix in vivo by using second-harmonic generation and two-photon excited fluorescence , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[11]  K. Reiser,et al.  Nonenzymatic Glycation of Collagen in Aging and Diabetes , 1998, Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine.

[12]  K. König,et al.  Multiphoton microscopy in life sciences , 2000, Journal of microscopy.

[13]  E. Georgiou,et al.  Thermally Induced Irreversible Conformational Changes in Collagen Probed by Optical Second Harmonic Generation and Laser-induced Fluorescence , 2002, Lasers in Medical Science.

[14]  E. Eikenberry,et al.  Glycation induces expansion of the molecular packing of collagen. , 1988, Journal of molecular biology.

[15]  W. Webb,et al.  Multiphoton microscopy in biological research. , 2001, Current opinion in chemical biology.

[16]  J. Eichler,et al.  Frequency doubling of ultrashort laser pulses in biological tissues. , 1999, Applied optics.

[17]  A J Bailey,et al.  Collagen cross-links in mineralizing tissues: a review of their chemistry, function, and clinical relevance. , 1998, Bone.