In vitro evaluation, molecular docking, and molecular dynamics studies of resorcinol derivatives against yeast α‐glucosidase

Ade Danova; Elvira Hermawati; Warinthorn Chavasiri; Didin Mujahidin; Iqbal Musthapa; Fera Kurniadewi

doi:10.22146/ijbiotech.106495

In vitro evaluation, molecular docking, and molecular dynamics studies of resorcinol derivatives against yeast α‐glucosidase

https://doi.org/10.22146/ijbiotech.106495

Ade Danova^(1*), Elvira Hermawati⁽²⁾, Warinthorn Chavasiri⁽³⁾, Didin Mujahidin⁽⁴⁾, Iqbal Musthapa⁽⁵⁾, Fera Kurniadewi⁽⁶⁾

(1) Organic Chemistry Division, Department of Chemistry, Faculty of Mathematics and Natural Sciences, Institut Teknologi Bandung, Jl. Ganesha 10, Bandung, West Java, 40132, Indonesia
(2) Organic Chemistry Division, Department of Chemistry, Faculty of Mathematics and Natural Sciences, Institut Teknologi Bandung, Jl. Ganesha 10, Bandung, West Java, 40132, Indonesia
(3) Center of Excellence in Natural Products Chemistry, Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330, Thailand
(4) Organic Chemistry Division, Department of Chemistry, Faculty of Mathematics and Natural Sciences, Institut Teknologi Bandung, Jl. Ganesha 10, Bandung, West Java, 40132, Indonesia
(5) Chemistry Study Program, Faculty of Mathematics and Natural Science Education, Universitas Pendidikan Indonesia, Jl. Dr. Setiabudi No 229, Bandung 40154, Indonesia
(6) Chemistry Study Program, Universitas Negeri Jakarta, Jalan Rawamangun Muka, Jakarta 13220, Indonesia
(*) Corresponding Author

Abstract

Nine resorcinol derivatives were evaluated for their ability to inhibit yeast α‐glucosidase using the in vitro method. Three molecular docking programs (Autodock Vina, Autodock4 and DockThor) were employed to determine the binding energies. The results showed that two resorcinol derivatives possessing butanoyl (1) and butyl (9) groups demonstrated good inhibitory activity against α‐glucosidase, with IC₅₀ values of 75.9 and 33.3 µM respectively, compared with other derivatives (2–8) and acarbose (IC₅₀ = 832.8 µM). Furthermore, molecular docking indicated that compounds 1 and 9 had better binding affinities than acarbose and the native ligand. Both compounds showed similar interactions with Asp349 and Glu408, which were associated with acarbose and the native ligand. Moreover, molecular dynamics analysis indicated that compound 9 exhibited greater stability than compound 1 when complexed with α‐glucosidase. Therefore, compound 9 has the potential for further studies, both in vitro and in vivo, to evaluate its toxicity, side effects and efficacy.

Keywords

α‐glucosidase inhibitors; Inhibitors; Molecular docking; Resorcinol

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References

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DOI: https://doi.org/10.22146/ijbiotech.106495