In silico docking studies of α-amylase inhibitors from the anti-diabetic plant Leucas ciliata Benth. and an endophyte, Streptomyces longisporoflavus .

Autor: Akshatha JV; Department of Studies in Botany, University of Mysore, Manasagangotri, Mysore, 570 006 Karnataka India., SantoshKumar HS; Department of Biotechnology, Bioscience Complex, Kuvempu University, JnanaSahyadri, Shankaraghatta, 577 451 Shivamogga, Karnataka India., Prakash HS; UGC-BSR Fellow, Department of Studies in Biotechnology, University of Mysore, Manasagangotri, Mysore, 570 006 Karnataka India., Nalini MS; Department of Studies in Botany, University of Mysore, Manasagangotri, Mysore, 570 006 Karnataka India.
Jazyk: angličtina
Zdroj: 3 Biotech [3 Biotech] 2021 Feb; Vol. 11 (2), pp. 51. Date of Electronic Publication: 2021 Jan 11.
DOI: 10.1007/s13205-020-02547-0
Abstrakt: In this investigation, potential inhibitors of α-amylase, one of the key regulatory enzymes in diabetes were characterized from the methanolic extract of Leucas ciliata Benth. (Lamiaceae), a traditional medicinal plant of the Western Ghats, southern India and the ethyl acetate extract of Streptomyces longisporoflavus (JX965948), an endophytic actinomycete isolated from the stem fragments of L. ciliata , by Gas Chromatography and Mass Spectroscopy (GC-MS) technique followed by molecular docking studies. Forty-four compounds were detected in the solvent extracts of the host plant and the endophyte, respectively. These compounds were selected as ligands for the receptor α-amylase in the molecular docking studies using PyRx software (0.8 V) for the inhibition of α-amylase activity. The ligands were ranked based on the binding energies ranging between - 3.1 and - 10.1 kcal/mol. Three ligands from the host plant extract, viz., Topotecan (PNo_7), Cathine (PNo_17) and 2,5-dimethoxy-4-(methylsulfonyl)amphetamine (PNo_18), depicted good binding energies of - 5.2 to - 7.8, respectively, whereas seven compounds from the endophyte extract showed binding energies in the range of - 4.7 to - 10.1, respectively. The standard α-amylase inhibitor Acarbose™ depicted binding energy of - 9.2 kcal/mol. All ligands were subjected to lead-likeliness property using Lipinski's rule of five. On the basis of the hydrogen bonding interactions with the receptor, and chemoinformatics analysis for drug-likeliness, one ligand, Topotecan (PNo_7) from the host plant was identified as the potential α-amylase inhibitor. This is the first attempt to identify alkaloid and flavonoid compounds as the α-amylase inhibitors from the host plant and its endophyte simultaneously. The molecular docking analyses presented in this study could lead to the development of potent α-amylase inhibitors helpful in the treatment of diabetes.
Supplementary Information: The online version of this article (10.1007/s13205-020-02547-0) contains supplementary material, which is available to authorized users.
Competing Interests: Conflict of interestsThe authors declare that there is no conflict of interest regarding the publication of this paper.
(© King Abdulaziz City for Science and Technology 2021.)
Databáze: MEDLINE
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