Synthesis and molecular docking studies of some new tetra-amide derivatives as new inhibitors of Maltase-Glucoamylase

• Published in: Journal of molecular structure Vol. 1180; pp. 556 - 563
• Main Authors: Mohammadi, Ali Asghar, Taheri, Salman, Sadr, Ahmad Shahir, Ghaderi, Peghman, Ahdenov, Reza
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 15.03.2019
• Subjects: Inhibitors of Maltase-Glucoamylase; Molecular docking; Multi-component reactions; Tetra-amide; Ugi reaction; Multi-component reactions; Ugi reaction; Molecular docking; Tetra-amide; Inhibitors of Maltase-Glucoamylase
• ISSN: 0022-2860; 1872-8014
• DOI: 10.1016/j.molstruc.2018.11.101

Tetra amide derivatives have been synthesized in good yields via a one-pot pseudo seven-component ugi reaction of terephthalaldehyde, with 2 molecules of amines, isocyanides and 2-(3-ethoxy-4-(ethoxycarbonyl)phenyl)acetic acid), and also by condensation of 1,4-phenylenediamine, with 2 molecules aldehyde, isocyanides and 2-(3-ethoxy-4-(ethoxycarbonyl)phenyl)acetic acid). All the newly synthesized compounds were screened for molecular docking studies. Molecular docking studies were carried out using the crystal structure of C-terminal and N-terminal Maltase-Glucoamylase enzyme. Some of the ugi adducts showed minimum binding energy and good affinity toward the active pocket of Maltase-Glucoamylase enzyme in comparison to acarbose as a standard Maltase-Glucoamylase inhibitor. •We have designed comfortable and simple green synthesis for the provide of novel tetra amide as a biological compound in the absence of catalysts in a one-pot pseudo seven-component reaction including 1 molecule terephthalaldehyde, 2 molecules isocyanides, 2 molecules amines, 2 molecules 2-(3-ethoxy-4-(ethoxycarbonyl)phenyl)acetic acid or 1 molecule phenylenediamine, 2 molecules isocyanide, 2 molecules aldehydes, 2 molecules 2-(3-ethoxy-4-(ethoxycarbonyl)phenyl) acetic acid) via ugi pseudo seven-component reaction.•We also report molecular docking study indicated that all of the herein reported compounds could snugly occupy the active site of N-terminal and C-terminal of Human Maltase-Glucoamylase, which could make them a plausible candidate for the target site.•We believe that this combination of features and great potential as an anti-diabetic drugs.