Tengku Nazmi, Tengku Kamilah and Aminudin, Nurul Iman and Hamzah, Nurasyikin
(2022)
Molecular docking and adme profiling of xanthorrhizol derivatives as hyaluronidase inhibitors.
In: 2nd IKMPB Online Symposium, Kuantan, Pahang.
(Unpublished)
Abstract
Hyaluronidase (Hyal) enzyme is one of the potential biological targets for the development of anti-inflammatory agents. Xanthorrhizol, a bisabolene sesquiterpenoid isolated from Curcuma xanthorrhiza has been reported showing anti-inflammatory activities against cyclooxygenase (COX), inducible nitric oxide synthase (iNOS), and interleukins (IL). However, the activity of xanthorrhizol as a Hyal inhibitor has not been exploited. In this study, a total of 26 xanthorrhizol derivatives having structural modifications at R1 - R4 scaffold were chosen. The molecular docking was performed to virtually screened their SAR activities towards Hyal while the ADME prediction was done to predict their pharmacokinetic profile. All derivatives bind to the active site of Hyal1 with binding energies ranging from -5.7 kcal/mol to -8.5 kcal/mol. Derivatives 24, and 14 having benzyloxy moiety at R1 position and polar moieties at R3 and R4 position showed lower binding energies (-8.3, and -7.9 kcal/mol, respectively) compared to apigenin, 28 and xanthorrhizol, 1. These derivatives also fulfilled all ADME and drug-likeness properties suggesting them as potential Hyal inhibitors. Through this work, the activity of xanthorrhizol derivatives against Hyal1 can be predicted and screened as a basis for future modifications of xanthorrhizol as potential Hyal inhibitor.
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