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Title: | Inhibition of copper-mediated aggregation of human γD-crystallin by Schiff bases |
Authors: | Chauhan, Priyanka Muralidharan, Sai Brinda Anand Babu, Velappan DATTA, DHRUBAJYOTI Pratihar, Sanjay Debnath, Joy Ghosh, Kalyan Sundar Dept. of Chemistry |
Keywords: | Inhibition of copper-mediated Schiff bases Schiff base Copper complex γD-Crystallin γD-Crystallin Purification of HGD 2017 |
Issue Date: | Jun-2017 |
Publisher: | Springer Nature |
Citation: | JBIC Journal of Biological Inorganic Chemistry, 22(4), 505-517. |
Abstract: | Protein aggregation, due to the imbalance in the concentration of Cu2+ and Zn2+ ions is found to be allied with various physiological disorders. Copper is known to promote the oxidative damage of β/γ-crystallins in aged eye lens and causes their aggregation leading to cataract. Therefore, synthesis of a small-molecule ‘chelator’ for Cu2+ with complementary antioxidant effect will find potential applications against aggregation of β/γ-crystallins. In this paper, we have reported the synthesis of different Schiff bases and studied their Cu2+ complexation ability (using UV–Vis, FT-IR and ESI-MS) and antioxidant activity. Further based on their copper complexation efficiency, Schiff bases were used to inhibit Cu2+-mediated aggregation of recombinant human γD-crystallin (HGD) and β/γ-crystallins (isolated from cataractous human eye lens). Among these synthesized molecules, compound 8 at a concentration of 100 μM had shown ~95% inhibition of copper (100 μM)-induced aggregation. Compound 8 also showed a positive cooperative effect at a concentration of 5–15 μM on the inhibitory activity of human αA-crystallin (HAA) during Cu2+-induced aggregation of HGD. It eventually inhibited the aggregation process by additional ~20%. However, ~50% inhibition of copper-mediated aggregation of β/γ-crystallins (isolated from cataractous human eye lens) was recorded by compound 8 (100 μM). Although the reductive aminated products of the imines showed better antioxidant activity due to their lower copper complexing ability, they were found to be non-effective against Cu2+-mediated aggregation of HGD. |
URI: | http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/3221 https://doi.org/10.1007/s00775-016-1433-0 |
ISSN: | 0949-8257 1432-1327 |
Appears in Collections: | JOURNAL ARTICLES |
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