The Potency of Catechin from Gambir (Uncaria gambir Roxb.) as a Natural Inhibitor of MurA (1UAE) Enzyme: In vitro and In silico studies

2020 ◽  
Vol 17 (12) ◽  
pp. 1531-1537
Author(s):  
Bella Riyana ◽  
Desi Harneti Putri Huspa ◽  
Mieke Hemiawati Satari ◽  
Dikdik Kurnia
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
In Silico ◽  
Bacterial Activity ◽  
Bacterial Cell Wall ◽  
Resistant Bacteria ◽  
In Silico Studies ◽  
In Silico Study ◽  
Natural Inhibitor

Background: Currently, infectious diseases caused by pathogenic and resistant bacteria are more challenging for anti-bacterial drug discovery. The discovery of new anti-bacterial agents developed in many mechanisms includes disruption of the bacterial cell wall formations. The MurA is a key enzyme contributing to the first step of bacterial peptidoglycan biosynthesis and is, therefore, proposed as an effective bactericidal target. Objective: The purpose of this research is to identify anti-bacterial compounds from U. gambir Roxb and to predict the potential inhibitory activities against murA enzyme by in silico study. Materials and Methods: Investigation and discovery of new inhibitors of MurA enzyme were conducted on the medicinal plant of Gambir (Uncaria gambir Roxb) and those that reportedly contained anti-bacterial agents. The anti-bacterial compounds were isolated by combinations of chromatography methods guided by anti-bacterial activity against bacteria of E. faecalis, S. mutans, and S. sanguinis. The structures of active compounds were characterized by spectroscopic methods, and the anti-bacterial activity was evaluated by the microdilution method (in vitro) combined with molecular docking of the MurA enzyme (in silico). Results: The anti-bacterial flavonoids of catechin were isolated from U. gambir Roxb with MIC values of 6250 and 12500 ppm, respectively, against S. sanguinis and E. faecalis. The in silico study showed that catechin has a binding affinity of -8.5 Kcal/mol to MurA which is higher than fosfomycin as a positive control. Conclusions: The catechin is predicted to have potential as a new natural inhibitor of the MurA enzyme to inhibit bacterial cell wall biosynthesis.

Potential Fatty Acid as Antibacterial Agent against Oral Bacteria of Streptococcus mutans and Streptococcus sanguinis from Basil (Ocimum americanum): In vitro and in silico studies.

2020 ◽  
Vol 17 ◽  
Author(s):  
Yetty Herdiyati ◽  
Yonada Astrid ◽  
Aldina Amalia Nur Shadrina ◽  
Ika Wiani ◽  
Mieke Hemiawati Satari ◽  
...  
Keyword(s):  
Cell Wall ◽  
Antibacterial Activity ◽  
Streptococcus Mutans ◽  
Lauric Acid ◽  
Bacterial Cell ◽  
In Silico ◽  
Antibacterial Agent ◽  
Bacterial Cell Wall ◽  
Ocimum Americanum

Background: Streptococcus mutans and Streptococcus sanguinis are Gram-positive bacteria that cause dental caries. The MurA enzyme is a catalyst in the formation of peptidoglycan in the bacterial cell wall making it ideal as an antibacterial target. Basil (Ocimum americanum) is an edible plant medicine that diverse, very widely spreading, used as herbal for a long time, and it was reported to have pharmacology effect as antibacterial activity. The purpose of this study is to identify antibacterial compounds from O. americanum and analyze their inhibition activity to the MurA enzyme. Methods: Fresh leaves from O. americanum extracted with n-hexane and purified by a combination of column chromatography on normal and reverse phase together with guided by in vitro bioactivity assay against S. mutans ATCC 25175 and S. sanguinis ATCC 10556, respectively, while in silico molecular docking simulation of lauric acid (1) using PyRx 0.8. Results: The structure determination of antibacterial compound by spectroscopic methods resulted in an active compound 1 as lauric acid. The in vitro evaluation of antibacterial activity compound 1 showed the MIC and MBC of 78.13 & 156.3 ppm and 1250 & 2500 ppm against S. sanguinis and in S. mutans, respectively. Further analysis in silico evaluation as MurA Enzyme inhibitor, lauric acid (1) has a binding affinity of -5.2 Kcal/mol those higher than fosfomycin. Conclusion: The lauric acid has potency as a new natural antibacterial agent through the MurA inhibition in bacterial cell wall biosynthesis.

Role of kallikrein-kinin system in pathogenesis of bacterial cell wall-induced inflammation

1991 ◽  
Vol 260 (2) ◽  
pp. G213-G219 ◽  
Author(s):  
R. A. DeLa Cadena ◽  
K. J. Laskin ◽  
R. A. Pixley ◽  
R. B. Sartor ◽  
J. H. Schwab ◽  
...  
Keyword(s):  
Cell Wall ◽  
Acute Phase ◽  
Bacterial Cell ◽  
Chronic Phase ◽  
Bacterial Cell Wall ◽  
Kinin System ◽  
Kallikrein Kinin System ◽  
Bacterial Products

The plasma kallikrein-kinin system is activated in Gram-negative sepsis and typhoid fever, two diseases in which bacterial products have been shown to initiate inflammation. Because a single intraperitoneal injection of bacterial cell wall peptidoglycan-polysaccharide polymers from group A steptococci (PG-APS) into a Lewis rat produces a syndrome of relapsing polyarthritis and anemia, we investigated changes in the role of the kallikrein-kinin system in this model of inflammation. Coagulation studies after injection of PG-APS revealed an immediate and persistent decrease in prekallikrein levels. High-molecular-weight kininogen levels decreased significantly during the acute phase and correlated with the severity of arthritis. Factor XI levels were decreased only during the acute phase. Antithrombin III levels remained unchanged, indicating that neither decreased hepatic synthesis nor disseminated intravascular coagulation caused the decreased plasma contact factors. Plasma T-kininogen (an acute phase protein) was significantly elevated during the chronic phase. PG-APS failed to activate the contact system in vitro. Thus the kallikrein-kinin system plays an important role in this experimental model of inflammation, suggesting that activation of this system may play a role in the pathogenesis of inflammatory bowel disease and rheumatoid arthritis in which bacterial products might be etiologically important.

SEQUENCE STUDIES ON BACTERIAL CELL WALL PEPTIDES

1964 ◽  
Vol 42 (11) ◽  
pp. 1553-1559 ◽  
Author(s):  
D. Jušić ◽  
C. Roy ◽  
R. W. Watson
Keyword(s):  
Cell Wall ◽  
Paper Chromatography ◽  
High Voltage ◽  
Bacterial Cell ◽  
Paper Electrophoresis ◽  
Bacterial Cell Wall ◽  
Molar Ratios

Peptides from partial acid hydrolysates of purified mucopeptide from Aerobacter cloacae NRC 492 were isolated by a combination of high-voltage paper electrophoresis and paper chromatography. Three dipeptides (L-ala.D-glu, D-glu.meso-Dap, and meso-Dap.D-ala), two tripeptides (ala.D-glu.meso-Dap and D-glu.meso-Dap.ala, i.e. D-glutamyl.meso-diaminopimelyl.alanine), and a tetrapeptide were partially characterized. Molar ratios, sequence, and optical configurations in a tripeptide from the wall corresponded with those in a uridine diphospho muramyl tripeptide from penicillin-treated cells of the same organism and with those of a tripeptide synthesized in vitro by enzymes from cell sonicates.

scholarly journals Antibacterial efficacy of Jackfruit rag extract against clinically important pathogens and validation of its antimicrobial activity in Shigella dysenteriae infected Drosophila melanogaster infection model

2020 ◽  
Author(s):  
NV Dhwani ◽  
Gayathri Raju ◽  
Sumi E Mathew ◽  
Gaurav Baranwal ◽  
Shivakumar B Shivaram ◽  
...  
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Antibacterial Property ◽  
Mouse Fibroblast ◽  
Bacterial Cell Wall ◽  
Shigella Dysenteriae ◽  
Infection Model ◽  
Bacterial Cells

AbstractThe aim of this study was to determine the antibacterial property of extract derived from a part of the Jackfruit called ‘rag’, that is generally considered as fruit waste. Morpho-physical characterization of the Jackfruit rag extract (JFRE) was performed using gas-chromatography, where peaks indicative of furfural; pentanoic acid; and hexadecanoic acid were observed. In vitro biocompatibility of JFRE was performed using the MTT assay, which showed comparable cellular viability between extract-treated and untreated mouse fibroblast cells. Agar well disc diffusion assay exhibited JFRE induced zones of inhibition for a wide variety of laboratory and clinical strains of gram-positive and gram-negative bacteria. Analysis of electron microscope images of bacterial cells suggests that JFRE induces cell death by disintegration of the bacterial cell wall and precipitating intracytoplasmic clumping. The antibacterial activity of the JFREs was further validated in vivo using Shigella dysenteriae infected fly model, where JFRE pre-fed flies infected with S. dysenteriae had significantly reduced mortality compared to controls. JFRE demonstrates broad antibacterial property, both in vitro and in vivo, possibly by its activity on bacterial cell wall. This study highlights the importance of exploring alternative sources of antibacterial compounds, especially from plant-derived waste, that could provide economical and effective solutions to current challenges in antimicrobial therapy.

scholarly journals Rutin as a Promising Inhibitor of Main Protease and Other Protein Targets of COVID-19: In Silico Study

2020 ◽  
Vol 15 (9) ◽  
pp. 1934578X2095395
Author(s):  
Ateeq Ahmed Al-Zahrani
Keyword(s):  
In Silico ◽  
Protein Targets ◽  
Main Protease ◽  
In Silico Studies ◽  
In Silico Study ◽  
Long Time ◽  
Formed Hydrogen ◽  
Homology Models

The process of investigating a possible cure for coronavirus disease 2019 (COVID-19) in vitro and in vivo may take a long time. For this reason, several in silico studies were performed in order to produce preliminary results that could lead to treatment. Extract of Juniperus procera Hochst is used as a traditional medicine for recovery from flu in Saudi Arabia. In the present study, more than 51 phytochemicals of J. procera were docked against the main protease of COVID-19. Rutin gave the highest interaction score among all the phytochemicals and the commercially available antiviral drugs. Lopinavir showed the second highest binding score. Rutin and lopinavir were further investigated using homology models of COVID-19. Rutin showed a better inhibition score in 9 of the 11 of homology models compared with lopinavir. Analysis of ligand-protein interaction contacts revealed that 3 residues (Glu166, Gly143, and Thr45) of the main protease formed hydrogen bonds with rutin. This simulation study suggests that rutin could be a possible effective inhibitor of several COVID-19 protein targets, including the main protease. Rutin, already available for commercial use, was evaluated for its ability as a possible drug. To our knowledge, this is the first study that suggests rutin having a possible strong inhibitory role against several protein targets of COVID-19.

scholarly journals The disruptive effect of lysozyme on the bacterial cell wall explored by an in-silico structural outlook

2017 ◽  
Vol 46 (1) ◽  
pp. 83-90 ◽  
Author(s):  
Emiliano D. Primo ◽  
Lisandro H. Otero ◽  
Francisco Ruiz ◽  
Sebastián Klinke ◽  
Walter Giordano
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
In Silico ◽  
Bacterial Cell Wall ◽  
Disruptive Effect
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