Rational Design, Synthesis, in Vitro, and in Silico Studies of Chlorophenylquinazolin‐4(3H)‐One Containing Different Aryl Acetohydrazides as Tyrosinase Inhibitors. Issue 7 (8th June 2022)

• Record Type: Journal Article
• Authors: Hajimiri, Mirhamed; Khosravikia, Mohammad; Khoshneviszadeh, Mehdi; Pedrood, Keyvan; Hosseini, Seyedeh Zahra; Asgari, Mohammad Sadegh; Pirhadi, Somayeh; Attarroshan, Mahshid; Mobaraki, Koroush; Hosseini, Samanesadat; Behnammanesh, Hossein; Biglar, Mahmood; Karimian, Somayeh; Rastegar, Hossein; Hamedifar, Haleh; Larijani, Bagher; Mahdavi, Mohammad; Iraji, Aida
• Is Part Of: Chemistry & biodiversity. Volume 19:Issue 7(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-06-08
• Subjects: quinazolines -- tyrosinase -- in silico -- synthesis -- structure-activity relationship; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Biodiversity -- Periodicals; 572
• DOI: 10.1002/cbdv.202100964
• Languages: English
• ISSNs: 1612-1872

Abstract

Abstract: Tyrosinase plays a pivotal role in the hyperpigmentation and enzymatic browning of fruit and vegetable. Therefore, tyrosinase inhibitors can be of interest in industries as depigmentation compounds as well as anti‐browning agents. In the present study, a series of chlorophenylquinazolin‐4(3 H )‐one derivative were rationally designed and synthesized. The formation of target compounds was confirmed by spectral characterization techniques such as IR, 1 H‐NMR, 13 C‐NMR, and elemental analysis. Among the synthesized derivatives, compound 8l was proved to be the most potent inhibitor with an IC50 value of 25.48±1.19 μM. Furthermore, the results of the molecular docking study showed that this compound fitted well in the active site of tyrosinase with the binding score of −10.72. Abstract :