2017
DOI: 10.1080/02713683.2017.1324628
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Effect of Green Tea Polyphenol Epigallocatechin-3-gallate on the Aggregation of αA(66-80) Peptide, a Major Fragment of αA-crystallin Involved in Cataract Development

Abstract: In the present study, we are able to successfully demonstrate that EGCG efficiently blocks the aggregation of αA(66-80) peptide in a concentration-dependent manner. Furthermore, it is also evident that EGCG is able to disaggregate pre-formed αA(66-80) aggregates. The study suggests that EGCG can be a potential molecule that can prevent the initiation of cataract as well as be helpful in the disease reversal.

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Cited by 12 publications
(11 citation statements)
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“…A variety of small molecules are known to inhibit fibrillation by affecting β-amyloid oligomerization, fibrillation or both (Necula et al, 2007;Porat et al, 2006). Fibrillation of αA 66−80 peptide itself was inhibited by epigallocatechin-3-gallate (Kumar et al, 2017) and fibrillation of HU γD-crystallin and bovine α-crystallin under denaturing conditions was blocked by certain dyes (Sharma and Ghosh, 2017), as well as by carnosine (Attanasio et al, 2009), respectively. In addition to reducing protein disulfide, DTT is known to interact with domains of proteins that lack cysteine residues (Alliegro, 2000), and thus the molecule may have been able to interfere with fibrillation via hydrogen bonding to the GP αAcrystallins.…”
Section: Discussionmentioning
confidence: 99%
“…A variety of small molecules are known to inhibit fibrillation by affecting β-amyloid oligomerization, fibrillation or both (Necula et al, 2007;Porat et al, 2006). Fibrillation of αA 66−80 peptide itself was inhibited by epigallocatechin-3-gallate (Kumar et al, 2017) and fibrillation of HU γD-crystallin and bovine α-crystallin under denaturing conditions was blocked by certain dyes (Sharma and Ghosh, 2017), as well as by carnosine (Attanasio et al, 2009), respectively. In addition to reducing protein disulfide, DTT is known to interact with domains of proteins that lack cysteine residues (Alliegro, 2000), and thus the molecule may have been able to interfere with fibrillation via hydrogen bonding to the GP αAcrystallins.…”
Section: Discussionmentioning
confidence: 99%
“…Moreover, a polyphenol derived from green tea, epigallocatechin-3-gallate (EGCG) attenuated and reversed the aggregation of αA (66)(67)(68)(69)(70)(71)(72)(73)(74)(75)(76)(77)(78)(79)(80), a peptide fragment derived from αA-crystallin peptide. Since αA (66)(67)(68)(69)(70)(71)(72)(73)(74)(75)(76)(77)(78)(79)(80) aggregates play a role in the destabilization of native crystallin structures, EGCG can potentially prevent onset and reverse cataract formation [122]. In corroboration, green tea (Camellia sinensis) leaf extract mitigated Na selenite-induced reduction on SOD, GSH-Px and CAT activities, and increase in lipid peroxidation in Wistar rat lenses, ex vivo [123].…”
Section: Plant-derived Compounds and Herbal Extractsmentioning
confidence: 89%
“…Moreover, a polyphenol derived from green tea, epigallocatechin-3-gallate (EGCG) attenuated and reversed the aggregation of αA(66-80), a peptide fragment derived from αA-crystallin peptide. Since αA(66-80) aggregates play a role in the destabilization of native crystallin structures, EGCG can potentially prevent onset and reverse cataract formation [122]. In corroboration, green tea (Camellia sinensis) leaf extract mitigated Na selenite-induced reduction on SOD, GSH-Px and CAT activities, and increase in lipid peroxidation in Wistar rat lenses, ex vivo [123].…”
Section: Plant-derived Compounds and Herbal Extractsmentioning
confidence: 89%
“…Human γcrystallin EGCG attenuated and reversed peroxide-induced aggregation of αA(66-80), a peptide fragment derived from αA-crystallin peptide [122] Green tea (Camellia sinensis) leaves extract Sodium selenite (100 µM)…”
Section: Wistar Rat Lensesmentioning
confidence: 99%