Antiglycation and enzyme inhibitory potential of salicylalazine isolated from Micromeria biflora (Buch.-Ham.ex D.Don) Benth

• Published in: South African journal of botany 2021-12, Vol.143, p.344-349
• Main Authors: Rauf, Abdur, Bawazeer, Saud, Rashid, Umer, El-Esawi, Mohamed A., Khan, Muhammad Humayun, Shah, Syed Uzair Ali, Mubarak, Mohammad S., Rengasamy, Kannan RR
• Format: Article
• Language: English
• Subjects: Antiglycation; Micromeria biflora; Phosphodiesterase; Tyrosinase; Urease
• ISSN: 0254-6299; 1727-9321
• DOI: 10.1016/j.sajb.2020.12.021

•The salicylalazine isolation from chloroform fraction of Micromeria biflora Benth.•Salicylalazine evaluation for (in vitro) inhibition of biological targets such as urease, phosphodiesterase-1, tyrosinase, and anti-glycation.•The results concluded that salicylalazine exhibits remarkable enzyme inhibition and anti-glycation effects. The aim of the present study was focused on experimental analysis for medicinal use of Micromeria biflora Benth. The plant was collected and subjected to extraction and fractionation; the chloroform fraction resulted in the isolation of a new constituent salicylalazine, using preparative HPLC. The Chemical structure of salicylalazine was confirmed through NMR and high-resolution mass spectrometry. Salicylalazine was evaluated (in vitro) against various biological targets such as urease, phosphodiesterase-1, tyrosinase, and anti-glycation studies. Furthermore, the binding orientation and interaction pattern of salicylalazine with crucial amino acid residues of the respective targets were used to explore the mechanism of enzymes inhibition. Results indicated that salicylalazine caused potent urease inhibition with an IC50 value of 12.4 ± 1.10 µM, in comparison of standard thiourea (IC50 = 21.0 ± 0.21 µM). The compound exhibited excellent inhibition potential against tyrosinase (89.4%), phosphodiesterase-1 (94.7%) compared to the standards kojic acid (86.3%) and EDTA (86.4%), respectively. Besides, salicylalazine possessed good anti-glycation activity with % inhibition of 86% and IC50 value of 248.7 ± 2.09 µM, compared to the standard Rutin (96%, IC50 value of 295 ± 3.14). Thus, it is concluded that salicylalazine, the active constituent Micromeria biflora Benth, exhibited remarkable in vitro inhibition of urease, phosphodiesterase-1, tyrosinase, and anti-glycation.