Birefringence effect studies of collagen formed by nonenzymatic glycation using dual-retarder Mueller polarimetry.

Abstract

.Significance: Nonenzymatic glycation of collagen covalently attaches an addition of sugar molecules that initially were involved in a reversibly reaction with amino groups on the protein. Due to the ultimate formation of stable irreversible advanced glycation end products, the process of glycation leads to abnormal irreversible cross-linking, which ultimately accumulates with age and/or diabetes in the extracellular matrix, altering its organization.Aim: We report the use of dual-retarder Mueller polarimetry in conjunction with phase retardance to differentiate collagen cross-linking in a normal collagen gel matrix from that in tissues with nonenzymatic cross-linking.Approach: A dual-liquid crystal-based Mueller polarimetry system that involves electronic modulation of polarization state generators (PSGs) was employed to produce all types of polarization states without moving any part and enable detection of the signal directly using a Stokes polarimeter. The linear phase retardance response was obtained for the characterization of the solution and gel forms of collagen using differential Mueller matrix analysis.Results: We found that linear phase retardance measurements via differential Mueller matrix polarimetry successfully differentiated collagen gel matrices with different degrees of cross-linking formed by a nonenzymatic glycation process and demonstrated that this technology constitutes a quick and simple modality.Conclusions: This approach has high sensitivity for studying differences in fibrillar cross-linking in glycated collagen. Further, our work suggests that this method of structural analysis has potential clinical diagnostic value owing to its noninvasive and cost-efficient nature.