Design, synthesis, α-amylase inhibition and in silico docking study of novel quinoline bearing proline derivatives

A new class of compounds formed by the linkage of −C(O)–NH– with pyridine and thiazole moieties was designed, synthesized, and characterized by various spectral approaches. The newly characterized compounds were evaluated for their antimicrobial as well as anti-inflammatory properties. The in vitro anti-inflammatory activity of these compounds was evaluated by denaturation of the bovine serum albumin method and showed inhibition in the range of IC 50 values—46.29–100.60 μg/mL. Among all the tested compounds, compound 5l has the highest IC 50 value and compound 5g has the least IC 50 value. On the other hand, antimicrobial results revealed that compound 5j showed the lowest MIC values and compound 5a has the highest MIC values. Furthermore, molecular docking of the active compounds demonstrated a better docking score and interacted well with the target protein. Physicochemical parameters of the titled compounds were found suitable in the reference range only. The in silico molecular docking study revealed their COX-inhibitory action. Compound 5j emerged as a significant bioactive molecule among the synthesized analogues.

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“…The RMSD value of the crystallographic orientation and the best docked pose was found to be 0.20 Å. 46 , 47 …”

Section: Experimental Sectionmentioning

confidence: 91%

Pyridine- and Thiazole-Based Hydrazides with Promising Anti-inflammatory and Antimicrobial Activities along with Their In Silico Studies

et al. 2020

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“…[33] Silicon method Molecular docking is a method used to predict the binding site and affinity of small ligand molecules at receptor macromolecular binding sites . [34][35][36][37] The docking process mainly involves spatial and energy matching between the ligand and the receptor to obtain the best conformation, and focuses on their compatibility. Molecular docking can also be used in the screening of αamylase inhibitors to determine whether the small inhibitors have an effect on amylase.…”

Section: Quick Determination Methodsmentioning

confidence: 99%

Proteinaceous α-amylase inhibitors: purification, detection methods, types and mechanisms

Zhou

Zhang

et al. 2021

International Journal of Food Properties

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α-Amylase is abundant in plants and animals. α-Amylase inhibitors can reduce endogenous α-amylase activity, playing an essential role in agricultural pest control, and preventing and treating human disease. In the agricultural field, α-Amylase inhibitors can restrict pest that relies on the starch of crops. Acarbose is an α-amylase inhibitor used to treat diabetes. Some αamylase inhibitors are represented by antinutritional factors, while others are proteinaceous. Depending on their structures and sources, researchers have divided them into seven types: The knottin-like type, the γ-thionin-like type, the cereal type, the Kunitz type, the thaumatin-like type, and the lectin-like type. This paper introduces the methods for separating, purifying, and detecting proteinaceous α-amylase inhibitors while examining the structure and inhibition mechanism of several proteinaceous α-amylase inhibitors. Finally, it explores the potential applications of α-amylase inhibitors.

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“…Oligosaccharides released in the digestion process are further hydrolyzed into an absorbable monosaccharide: glucose. Glucose absorption into the bloodstream in patients with insulin disorders causes a sharp increase in the blood glucose level, which may lead to development of the disease [11]. Peptides with enzyme inhibitory activity involved in polysaccharide metabolism and exhibiting a potent anti-diabetic effect were described previously: CSSV, YSPR, SAAP, PGGP, and LGGGNT [12], or LPLLR [13] Fats are energy-delivering molecules.…”

Section: Introductionmentioning

confidence: 99%

Characteristics of New Peptides GQLGEHGGAGMG, GEHGGAGMGGGQFQPV, EQGFLPGPEESGR, RLARAGLAQ, YGNPVGGVGH, and GNPVGGVGHGTTGT as Inhibitors of Enzymes Involved in Metabolic Syndrome and Antimicrobial Potential

et al. 2020

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The aim of this study was to determine the cytotoxic properties, influence on enzyme activity involved in metabolic syndrome, and antimicrobial activity of synthetic peptides with GQLGEHGGAGMG, GEHGGAGMGGGQFQPV, EQGFLPGPEESGR, RLARAGLAQ, YGNPVGGVGH, and GNPVGGVGHGTTGT sequences. Peptides have no cytotoxic effect on cells. The highest inhibitory effect on angiotensin converting enzyme I was noted for peptide GT-14 (IC50 = 525.63 µg/mL). None of the tested peptides had an influence on α-glucosidase. The highest α-amylase and lipase inhibitory activity was noted for GG-12 (IC50 = 56.72 and 60.62 µg/mL, respectively). The highest lipoxidase inhibitory activity was determined for peptide ER-13 (IC50 = 84.35 µg/mL). Peptide RQ-9 was characterized by the highest COX inhibitory activity (0.31 and 4.77 µg/mL for COX-1 and COX-2, respectively). Only peptide RQ-9 inhibited S. enteritidis ATCC 4931 growth (42–48%) in all tested concentrations (15.62–250 mg/mL).

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Design, synthesis, α-amylase inhibition and in silico docking study of novel quinoline bearing proline derivatives

Cited by 35 publications

References 39 publications

Pyridine- and Thiazole-Based Hydrazides with Promising Anti-inflammatory and Antimicrobial Activities along with Their In Silico Studies

Pyridine- and Thiazole-Based Hydrazides with Promising Anti-inflammatory and Antimicrobial Activities along with Their In Silico Studies

Proteinaceous α-amylase inhibitors: purification, detection methods, types and mechanisms

Characteristics of New Peptides GQLGEHGGAGMG, GEHGGAGMGGGQFQPV, EQGFLPGPEESGR, RLARAGLAQ, YGNPVGGVGH, and GNPVGGVGHGTTGT as Inhibitors of Enzymes Involved in Metabolic Syndrome and Antimicrobial Potential

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