Progressive changes in secondary conformation and composition of the senile cataractous human lens capsules
| Autor: | Run-Chu Liang, Shan-Yang Lin, Shui-Mei Lee, Ching‐Li Cheng |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Adult
Male Aging Lens Capsule Crystalline Cataract Protein Structure Secondary Protein structure Optics Spectroscopy Fourier Transform Infrared medicine Humans Eye Proteins Protein secondary structure Aged business.industry Disease progression Middle Aged Ophthalmology medicine.anatomical_structure Structural composition Lens (anatomy) Disease Progression Biophysics Composition (visual arts) Cataractous lens business Algorithms Triple helix |
| Zdroj: | Acta Ophthalmologica Scandinavica. 74:542-546 |
| ISSN: | 1395-3907 |
| DOI: | 10.1111/j.1600-0420.1996.tb00731.x |
| Popis: | The lens capsules of senile cataractous patients were differentiated into three progressive grades of immature (I, II and III) and two progressive grades of mature (I' and II') groups using Fourier transform infrared (FT-IR) microspectroscopy with Fourier self-deconvolution and curve-fitting algorithms, according to the changes in IR peak position and its structural composition. The secondary conformation of both immature-II and mature-I' cataractous human lens capsules was found to change significantly when enhancing the beta-sheet structure but simultaneously decreasing the beta-turn structures, as compared with the composition of normal human and immature-I cataractous lens capsules. The increase in beta-sheet structural proportion might possibly be attributable to the age-related cataractogenesis. We also found that the IR peak at 1651 cm-1 assigned to a-helix shifted to 1647 cm-1 that corresponded to disordered structure, but the IR peak at 1662 cm-1 due to beta-turn structure disappeared and another new IR peak assigned to alpha-helix structure appeared at 1656 cm-1, for both immature-III and mature-II' cataractous lens capsules. It increased the compositions of beta-sheet and disorder structures and simultaneously decreased the triple helix and beta-turn structures, but maintained the same level in alpha-helix structure. This suggests that FT-IR microspectroscopy can act as a potential tool to exactly differentiate the maturity of senile cataractous human lens capsules according to the changes in IR peak position and compositions in amide I band. |
| Databáze: | OpenAIRE |
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