Binding Model of Antidiabetic Constituents from Capsosiphon fulvescens with Human Aldose Reductase by Ogunwa Tomisin Happy in Open Access Journal of Biomedical Engineering and Biosciences (OAJBEB) - Lupine Publishers
The use of seaweeds as functional foods and drugs is well known. Capsosiphon fulvescens (C. fulvescens) is a green sea alga for which beneficial health impacts have been reported even in diabetes. In the present study, three C. fulvescens constituents (chalinasterol, capsofulvesin A and capsofulvesin B) were evaluated for their molecular binding signature and interaction patterns against human aldose reductase as an antidiabetic target. The enzyme has been robustly implicated in the development of secondary complications of diabetes. The results generated here with the aid of in silico tools revealed a favourable binding affinity for the seawed constituents on the active site of aldose reductase. However, detailed observation shows no interference with the NADP binding pocket. The binding configuration of capsofulvesin A and capsofulvesin B were comparable to fidarestatas the compounds inserted one of their elongated aliphatic long chains with double bonds into the binding pocket. Nonetheless, subtle differences were sighted with the binding format of the aliphatic chain of capsofulvesin B resulting from a possible hydrophobic hinderance or influence within the binding pocket. Only one of the aliphatic chains of capsofulvesin A enjoyed hydrophobic interaction with residues Val47, Trp219 and Phe122 compared to the capsofulvesin B having hydrophobic interaction with Phe122 at the second chain while the other aliphatic chain formed hydrophobic bond with Trp20, Val47, Trp219 and Leu300. Meanwhile, the galactose unit of the two compounds displayed similar binding orientation and interaction with amino acid residues Ser22 and Trp20 at the active site. Chalinasterol, on the other hand, established hydrogen bond with the imidazole ring of His110 and indole ring of Trp111 respectively. The current study represents the first attempt to model the interaction of these ligands with aldose reductase and the unique binding patterns might explain the mechanism and potency of C. fulvescens in the management of diabetes and its complications - Lupine Publishers.
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The use of seaweeds as functional foods and drugs is well known. Capsosiphon fulvescens (C. fulvescens) is a green sea alga for which beneficial health impacts have been reported even in diabetes. In the present study, three C. fulvescens constituents (chalinasterol, capsofulvesin A and capsofulvesin B) were evaluated for their molecular binding signature and interaction patterns against human aldose reductase as an antidiabetic target. The enzyme has been robustly implicated in the development of secondary complications of diabetes. The results generated here with the aid of in silico tools revealed a favourable binding affinity for the seawed constituents on the active site of aldose reductase. However, detailed observation shows no interference with the NADP binding pocket. The binding configuration of capsofulvesin A and capsofulvesin B were comparable to fidarestatas the compounds inserted one of their elongated aliphatic long chains with double bonds into the binding pocket. Nonetheless, subtle differences were sighted with the binding format of the aliphatic chain of capsofulvesin B resulting from a possible hydrophobic hinderance or influence within the binding pocket. Only one of the aliphatic chains of capsofulvesin A enjoyed hydrophobic interaction with residues Val47, Trp219 and Phe122 compared to the capsofulvesin B having hydrophobic interaction with Phe122 at the second chain while the other aliphatic chain formed hydrophobic bond with Trp20, Val47, Trp219 and Leu300. Meanwhile, the galactose unit of the two compounds displayed similar binding orientation and interaction with amino acid residues Ser22 and Trp20 at the active site. Chalinasterol, on the other hand, established hydrogen bond with the imidazole ring of His110 and indole ring of Trp111 respectively. The current study represents the first attempt to model the interaction of these ligands with aldose reductase and the unique binding patterns might explain the mechanism and potency of C. fulvescens in the management of diabetes and its complications - Lupine Publishers.
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https://lupinepublishers.com/biomedical-sciences-journal/fulltext/binding-model-of-antidiabetic-constituents-from-capsosiphon-fulvescens-with-human-aldose-reductase.ID.000110.php
https://lupinepublishers.com/biomedical-sciences-journal/abstracts/binding-model-of-antidiabetic-constituents-from-capsosiphon-fulvescens-with-human-aldose-reductase.ID.000110.phphttps://lupinepublishers.com/biomedical-sciences-journal/pdf/OAJBEB.MS.ID.000110.pdf
https://lupinepublishers.com/biomedical-sciences-journal/abstracts/binding-model-of-antidiabetic-constituents-from-capsosiphon-fulvescens-with-human-aldose-reductase.ID.000110.phphttps://lupinepublishers.com/biomedical-sciences-journal/pdf/OAJBEB.MS.ID.000110.pdf
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