Diaryl azo derivatives as anti-diabetic and antimicrobial agents: synthesis, in vitro, kinetic and docking studies. (1st January 2021)

• Record Type: Journal Article
• Authors: Tahir, Tehreem; Shahzad, Mirza Imran; Tabassum, Rukhsana; Rafiq, Muhammad; Ashfaq, Muhammad; Hassan, Mubashir; Kotwica-Mojzych, Katarzyna; Mojzych, Mariusz
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 36:Number 1(2021)
• Page Start: 1508
• Page End: 1519
• Publication Date: 2021-01-01
• Subjects: Antibacterial -- anti-diabetic -- azo derivatives -- molecular docking -- phenolic compounds; Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.1080/14756366.2021.1929949
• Languages: English
• ISSNs: 1475-6366

Abstract

Abstract: In the present study, a series of azo derivatives (TR-1 to TR-9 ) have been synthesised via the diazo-coupling approach between substituted aromatic amines with phenol or naphthol derivatives. The compounds were evaluated for their therapeutic applications against alpha-glucosidase (anti-diabetic) and pathogenic bacterial strains E. coli (gram-negative), S. aureus (gram-positive), S. aureus (gram-positive) drug-resistant strain, P. aeruginosa (gram-negative), P. aeruginosa (gram-negative) drug-resistant strain and P. vulgaris (gram-negative). The IC50 (µg/mL) of TR-1 was found to be most effective (15.70 ± 1.3 µg/mL) compared to the reference drug acarbose (21.59 ± 1.5 µg/mL), hence, it was further selected for the kinetic studies in order to illustrate the mechanism of inhibition. The enzyme inhibitory kinetics and mode of binding for the most active inhibitor (TR-1 ) was performed which showed that the compound is a non-competitive inhibitor and effectively inhibits the target enzyme by binding to its binuclear active site reversibly.