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- W3165606555 endingPage "120023" @default.
- W3165606555 startingPage "120023" @default.
- W3165606555 abstract "Cataract is known as one of the leading causes of vision impairment worldwide. While the detailed mechanism of cataratogenesis remains unclear, cataract is believed to be correlated with the aggregation and/or misfolding of human ocular lens proteins called crystallins. A 173-residue structural protein human γD-crystallin is a major γ-crystallin protein in the human eye lens and associated with the development of juvenile and mature-onset cataracts. This work is aimed at investigating the effect of a small molecule, e.g., ortho-vanillin, on human γD-crystallin aggregation upon exposure to ultraviolet-C irradiation. According to the findings of right-angle light scattering, transmission electron microscopy, and gel electrophoresis, ortho-vanillin was demonstrated to dose-dependently suppress ultraviolet-C-triggered aggregation of human γD-crystallin. Results from the synchronous fluorescence spectroscopy, tryptophan fluorescence quenching, and molecular docking studies revealed the structural change of γD-crystallin induced by the interaction/binding between ortho-vanillin and protein. We believe the outcome from this work may contribute to the development of potential therapeutics for cataract." @default.
- W3165606555 created "2021-06-07" @default.
- W3165606555 creator A5030268205 @default.
- W3165606555 creator A5032083553 @default.
- W3165606555 creator A5039482466 @default.
- W3165606555 creator A5059230162 @default.
- W3165606555 creator A5070275634 @default.
- W3165606555 date "2021-11-01" @default.
- W3165606555 modified "2023-10-17" @default.
- W3165606555 title "Protection of human γD-crystallin protein from ultraviolet C-induced aggregation by ortho-vanillin" @default.
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