Počet záznamů: 1
Determination of tyrosinase-cyanidin-3-O-glucoside and (-/ plus )-catechin binding modes reveal mechanistic differences in tyrosinase inhibition
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SYSNO ASEP 0551538 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Determination of tyrosinase-cyanidin-3-O-glucoside and (-/ plus )-catechin binding modes reveal mechanistic differences in tyrosinase inhibition Tvůrce(i) Lee, K. (KR)
Bharadwaj, Shiv (BTO-N)
Sahoo, A. (IN)
Yadava, U. (IN)
Kang, S. (KR)Celkový počet autorů 5 Číslo článku 24494 Zdroj.dok. Scientific Reports. - : Nature Publishing Group - ISSN 2045-2322
Roč. 11, č. 1 (2021)Poč.str. 25 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova mushroom tyrosinase ; cyclic voltammetry ; essential dynamics ; melanin synthesis ; crystal-structure Vědní obor RIV EB - Genetika a molekulární biologie Obor OECD 1.7 Other natural sciences Způsob publikování Open access Institucionální podpora BTO-N - RVO:86652036 UT WOS 000736780900007 DOI 10.1038/s41598-021-03569-1 Anotace Tyrosinase, exquisitely catalyzes the phenolic compounds into brown or black pigment, inhibition is used as a treatment for dermatological or neurodegenerative disorders. Natural products, such as cyanidin-3-O-glucoside and (-/+)-catechin, are considered safe and non-toxic food additives in tyrosinase inhibition but their ambiguous inhibitory mechanism against tyrosinase is still elusive. Thus, we presented the mechanistic insights into tyrosinase with cyanidin-3-O-glucoside and (-/+)-catechin using computational simulations and in vitro assessment. Initial molecular docking results predicted ideal docked poses (- 9.346 to 5.795 kcal/mol) for tyrosinase with selected flavonoids. Furthermore, 100 ns molecular dynamics simulations and post-simulation analysis of docked poses established their stability and oxidation of flavonoids as substrate by tyrosinase. Particularly, metal chelation via catechol group linked with the free 3-OH group on the unconjugated dihydropyran heterocycle chain was elucidated to contribute to tyrosinase inhibition by (-/+)-catechin against cyanidin-3-O-glucoside. Also, predicted binding free energy using molecular mechanics/generalized Born surface area for each docked pose was consistent with in vitro enzyme inhibition for both mushroom and murine tyrosinases. Conclusively, (-/+)-catechin was observed for substantial tyrosinase inhibition and advocated for further investigation for drug development against tyrosinase-associated diseases. Pracoviště Biotechnologický ústav Kontakt Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700 Rok sběru 2022 Elektronická adresa https://www.nature.com/articles/s41598-021-03569-1
Počet záznamů: 1