Biological effects of bis-hydrazone compounds bearing isovanillin moiety on the aldose reductase

• Published in: Bioorganic chemistry Vol. 117; pp. 105473 - 105487
• Main Authors: Yapar, Gönül, Esra Duran, Hatice, Lolak, Nebih, Akocak, Suleyman, Türkeş, Cüneyt, Durgun, Mustafa, Işık, Mesut, Beydemir, Şükrü
• Format: Journal Article
• Language: English
• Published: SAN DIEGO Elsevier Inc 01.12.2021; Elsevier
• Subjects: ADME-Tox; Aldehyde Reductase - antagonists & inhibitors; Aldehyde Reductase - metabolism; Aldose reductase; Benzaldehydes - chemistry; Benzaldehydes - pharmacology; Biochemistry & Molecular Biology; Bis-hydrazones; Chemistry; Chemistry, Organic; Dose-Response Relationship, Drug; Enzyme Inhibitors - chemical synthesis; Enzyme Inhibitors - chemistry; Enzyme Inhibitors - pharmacology; Epalrestat; Humans; Hydrazones - chemical synthesis; Hydrazones - chemistry; Hydrazones - pharmacology; In silico study; Life Sciences & Biomedicine; Molecular Docking Simulation; Molecular Structure; Physical Sciences; Science & Technology; Structure-Activity Relationship; ADME-Tox; Epalrestat; Aldose reductase; Bis-hydrazones; In silico study; VITRO; CARBONIC-ANHYDRASE I; PHENOLIC-COMPOUNDS; INHIBITORY-ACTIVITY; SILICO EVALUATION; CALCIUM-CHANNEL BLOCKERS; MOLECULAR DOCKING; POTENTIAL ACETYLCHOLINESTERASE; VII; HISTAMINE SCHIFF-BASES

[Display omitted] •The synthesis of a series of novel macrocyclic hydrazone compounds bearing isovanilline moiety (GY1-12) was reported.•ALR2 enzyme was purified with 2.99% yield and 2.10 EU/mg specific activity.•All compounds exhibited a high inhibitory effect on ALR2 as competitive and non-competi...