Protein size resolution in human eye lenses by dynamic light scattering after in vivo measurements: first analysis of a clinical validation

Karsten Dierks; Matthias Dieckmann; Dirk Niederstrasser; R. Schwartz; Alfred R. Wegener

doi:10.1117/12.199260

12 January 1995 Protein size resolution in human eye lenses by dynamic light scattering after in vivo measurements: first analysis of a clinical validation

Karsten Dierks, Matthias Dieckmann, Dirk Niederstrasser, R. Schwartz, Alfred R. Wegener

Author Affiliations +

Proceedings Volume 2330, Lasers in Ophthalmology II; (1995) https://doi.org/10.1117/12.199260
Event: International Symposium on Biomedical Optics Europe '94, 1994, Lille, France

Abstract

Laser light source powers of our instrument LEPOSIA^R are minimized so that dynamic light scattering (DLS) measurements can be conducted with lowest intensity levels on human eye lenses (3.2 mW/cm²) within measurement times of 3 to 5 seconds. We describe an extension of DLS and an eye lens characterization along the optical axis (OA), revealing the molecular size ranges together with distributions found in lens regions parallel to the OA. The microstructures of various lens regions are separated by the analyzed radius distributions reflecting the visco-elastic properties of the eye lens. Detailed analysis and applied statistical categorization of results are described. The data obtained by DLS allow for an objective interpretation of opacity occurrences on molecular size range which are related to refraction anomalies. Apart from changes in color and fluorescence properties, the refractive anomalies can be assumed as the origin of the cataract. The bimodal radius distributions are characterized as a function of patient ages varying from 9 to 85 years. Our clinical study on 42 subjects proves a size decrease of the monomeric fraction with age, whereby their relative frequency of occurrence decreases. The larger polymeric radius fractions which are detected in lenses of all subjects increase with their age. An increase of protein polymer size is likely to be linked to the decrease of the (gamma) -crystallin fraction in old eye lens nuclei. Our preliminary analysis of clinical results is corresponding to the chemical gradients parallel to the OA of the lenses which are reported by O. Hockwin after examination on extracted eye lenses. The normalization of the lens densitometric data derived after Scheimpflug- photography against the protein size fraction analysis by DLS is performed. As a comparison mean between both techniques on identical eye lenses, an absorption corrected densitometry is conducted for the first time.

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Karsten Dierks, Matthias Dieckmann, Dirk Niederstrasser, R. Schwartz, and Alfred R. Wegener "Protein size resolution in human eye lenses by dynamic light scattering after in vivo measurements: first analysis of a clinical validation", Proc. SPIE 2330, Lasers in Ophthalmology II, (12 January 1995); https://doi.org/10.1117/12.199260

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