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Spectrochim Acta A Mol Biomol Spectrosc ; 192: 318-327, 2018 Mar 05.
Article in English | MEDLINE | ID: mdl-29172128

ABSTRACT

Aggregation of human ocular lens proteins, the crystallins is believed to be one of the key reasons for age-onset cataract. Previous studies have shown that human γD-crystallin forms amyloid like fibres under conditions of low pH and elevated temperature. In this article, we have investigated the aggregation propensity of human γB-crystallin in absence and presence of epigallocatechin gallate (EGCG), in vitro, when exposed to stressful conditions. We have used different spectroscopic and microscopic techniques to elucidate the inhibitory effect of EGCG towards aggregation. The experimental results have been substantiated by molecular dynamics simulation studies. We have shown that EGCG possesses inhibitory potency against the aggregation of human γB-crystallin at low pH and elevated temperature.


Subject(s)
Catechin/analogs & derivatives , Computer Simulation , Protein Aggregates/drug effects , gamma-Crystallins/chemistry , gamma-Crystallins/ultrastructure , Amino Acid Motifs , Amino Acids/chemistry , Benzothiazoles , Catechin/pharmacology , Circular Dichroism , Humans , Hydrogen-Ion Concentration , Hydrophobic and Hydrophilic Interactions , Kinetics , Nephelometry and Turbidimetry , Protein Structure, Tertiary , Solutions , Spectrometry, Fluorescence , Thiazoles/chemistry
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