Abstract
ABSTRACTPolarized radiation is used in a Fourier transform infrared (FTIR) microspectroscopic technique to detect molecular conformational change in collagen fibers resulting from deterioration. Absorbance spectra of single fibers are produced with polarization oriented first parallel (A‖) and then perpendicular (A⊥) to the fiber axis. The amide Ill band (1230- 1300 cm−1) shows strong positive dichroism, with up to six times greater absorbance occurring with parallel polarization. Losses of dichroism result from breakdown in the molecular structure of collagen. Integrations of the amide III bands are used in ratios, A‖/A⊥;, which provide a measure of the degree of molecular order. Ratios for degraded and undegraded material are compared to produce semi-quantitative information about deterioration.
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