Exploring the in vitro anti-diabetic potential and in silico studies of 2, 3 and 2, 6-dichloroIndolinone DOI Creative Commons
Abdur Rauf, Waqas Alam, Momin Khan

и другие.

Drug Target Insights, Год журнала: 2025, Номер 19(1), С. 11 - 17

Опубликована: Март 10, 2025

Adequate hyperglycemic control is still a huge challenge with the clinically used therapeutics. New, more effective anti-diabetic agents are on top list of drug discovery projects. This article deals in vitro potential 2, 3 dichloroIndolinone (C1) and 6-dichloroIndolinone (C2) α-glucosidase α-amylase followed by silico analysis. Both compounds, C-1 C-2, caused significant inhibition at various test concentrations IC50 35.266 μM 38. 379 μM, respectively. Similarly, compounds C-2 elicited anti-α-amylase action values 42.449 46.708 The molecular docking investigation regarding binding site was implemented to attain better comprehension respect pattern which mechanics occur between C1 C2 molecules active sites, illustrated higher efficacy appraisal reference inhibitor acarbose. interactions residues were mainly polar bonds, hydrogen bonding, π-π, π-H interactions, contributed strong alignment enzyme backbone. frequently indicated stable hydrogen-bonding pattern, suggested minimal fluctuation MM-PBSA values. In short, this study will contribute providing these an improved profile decreased toxicity.

Язык: Английский

Exploring the in vitro anti-diabetic potential and in silico studies of 2, 3 and 2, 6-dichloroIndolinone DOI Creative Commons
Abdur Rauf, Waqas Alam, Momin Khan

и другие.

Drug Target Insights, Год журнала: 2025, Номер 19(1), С. 11 - 17

Опубликована: Март 10, 2025

Adequate hyperglycemic control is still a huge challenge with the clinically used therapeutics. New, more effective anti-diabetic agents are on top list of drug discovery projects. This article deals in vitro potential 2, 3 dichloroIndolinone (C1) and 6-dichloroIndolinone (C2) α-glucosidase α-amylase followed by silico analysis. Both compounds, C-1 C-2, caused significant inhibition at various test concentrations IC50 35.266 μM 38. 379 μM, respectively. Similarly, compounds C-2 elicited anti-α-amylase action values 42.449 46.708 The molecular docking investigation regarding binding site was implemented to attain better comprehension respect pattern which mechanics occur between C1 C2 molecules active sites, illustrated higher efficacy appraisal reference inhibitor acarbose. interactions residues were mainly polar bonds, hydrogen bonding, π-π, π-H interactions, contributed strong alignment enzyme backbone. frequently indicated stable hydrogen-bonding pattern, suggested minimal fluctuation MM-PBSA values. In short, this study will contribute providing these an improved profile decreased toxicity.

Язык: Английский

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