https://scholars.lib.ntu.edu.tw/handle/123456789/576781
標題: | Protection of human γD-crystallin protein from ultraviolet C-induced aggregation by ortho-vanillin | 作者: | Hsueh S.-S Lu J.-H Wu J.W Lin T.-H Wang S.S.-S. STEVEN SHENG-SHIH WANG |
公開日期: | 2021 | 卷: | 261 | 來源出版物: | Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy | 摘要: | 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. ? 2021 Elsevier B.V. |
URI: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85107666120&doi=10.1016%2fj.saa.2021.120023&partnerID=40&md5=d9e8d230089613a4457c2e3acf1491e1 https://scholars.lib.ntu.edu.tw/handle/123456789/576781 |
ISSN: | 13861425 | DOI: | 10.1016/j.saa.2021.120023 |
顯示於: | 化學工程學系 |
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