scholarly journals A Review on Platensimycin: A Selective FabF Inhibitor

2016 ◽  
Vol 2016 ◽  
pp. 1-16 ◽  
Author(s):  
Manik Das ◽  
Partha Sakha Ghosh ◽  
Kuntal Manna
Keyword(s):  
Antibacterial Activity ◽  
Bacterial Infection ◽  
Secondary Metabolite ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Structural Pattern ◽  
Gram Positive Bacteria ◽  
Streptomyces Platensis ◽  
Naturally Occurring ◽  
Retrosynthetic Analysis

Emerging resistance to existing antibiotics is an inevitable matter of concern in the treatment of bacterial infection. Naturally occurring unique class of natural antibiotic, platensimycin, a secondary metabolite from Streptomyces platensis, is an excellent breakthrough in recent antibiotic research with unique structural pattern and significant antibacterial activity. β-Ketoacyl-(acyl-carrier-protein (ACP)) synthase (FabF) whose Gram-positive bacteria need to biosynthesize cell membranes is the target of inhibition of platensimycin. So, isolation, retrosynthetic analysis, synthesis of platensimycin, and analogues of platensimycin synthesized till today are the objectives of this review which may be helpful to further investigate and to reveal untouched area on this molecule and to obtain a potential antibacterial lead with enhanced significant antibacterial activity.

scholarly journals Introducing Broadened Antibacterial Activity to Rhodanine Derivatives Targeting Enoyl-Acyl Carrier Protein Reductase

2019 ◽  
Vol 67 (2) ◽  
pp. 125-129
Author(s):  
Zhi-Gang Sun ◽  
Yun-Jie Xu ◽  
Jian-Fei Xu ◽  
Qi-Xing Liu ◽  
Yu-Shun Yang ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Acyl Carrier Protein ◽  
Carrier Protein

scholarly journals Katanosin B and Plusbacin A3, Inhibitors of Peptidoglycan Synthesis in Methicillin-ResistantStaphylococcus aureus

2001 ◽  
Vol 45 (6) ◽  
pp. 1823-1827 ◽  
Author(s):  
Hideki Maki ◽  
Kenji Miura ◽  
Yoshinori Yamano
Keyword(s):  
Cell Wall ◽  
Antibacterial Activity ◽  
Whole Cells ◽  
Gram Positive Bacteria ◽  
Peptidoglycan Synthesis ◽  
Cyclic Depsipeptide ◽  
Naturally Occurring ◽  
Vancomycin Resistant Enterococci ◽  
Vancomycin Resistant

ABSTRACT Both katanosin B and plusbacin A3 are naturally occurring cyclic depsipeptide antibiotics containing a lactone linkage. They showed strong antibacterial activity against methicillin-resistantStaphylococcus aureus and VanA-type vancomycin-resistant enterococci, with MICs ranging from 0.39 to 3.13 μg/ml, as well as against other gram-positive bacteria. They inhibited the incorporation of N-acetylglucosamine, a precursor of cell wall synthesis, into peptidoglycan of S. aureus whole cells at concentrations close to their MICs. In vitro studies with a wall-membrane particulate fraction of S. aureus showed that katanosin B and plusbacin A3 inhibited the formation of lipid intermediates, with 50% inhibitory concentrations (IC50s) of 2.2 and 2.3 μg/ml, respectively, and inhibited the formation of nascent peptidoglycan, with IC50s of 0.8 and 0.4 μg/ml, respectively. Vancomycin, a well-known inhibitor of transglycosylation, did not inhibit the formation of lipid intermediates but did inhibit the formation of nascent peptidoglycan, with an IC50 of 4.1 μg/ml. Acetyl-Lys-d-Ala-d-Ala, an analog of the terminus of the lipid intermediates, effectively suppressed the inhibition of transglycosylation by vancomycin, but did not suppress those by katanosin B and plusbacin A3. These results indicate that the antibacterial activity of katanosin B and plusbacin A3 is due to blocking of transglycosylation and its foregoing steps of cell wall peptidoglycan synthesis via a mechanism differing from that of vancomycin.

scholarly journals Antibacterial Activity of N-Pentylpantothenamide Is Due to Inhibition of Coenzyme A Synthesis

2010 ◽  
Vol 54 (3) ◽  
pp. 1374-1377 ◽  
Author(s):  
Jacob Thomas ◽  
John E. Cronan
Keyword(s):  
Antibacterial Activity ◽  
Growth Inhibition ◽  
Coenzyme A ◽  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Prosthetic Group ◽  
Protein Moiety

ABSTRACT Growth inhibition by the pantothenate analog N-pentylpantothenamide (N5-Pan) has been attributed to the accumulation of acyl carrier protein carrying a prosthetic group modified by incorporation of N5-Pan. This was attributed to an inability of the AcpH acyl carrier protein phosphodiesterase to cleave the N5-Pan-modified prosthetic group from the protein moiety. We report that AcpH readily removes the N5-Pan-modified prosthetic group both in vivo and in vitro and show that N5-Pan blocks coenzyme A synthesis.

Antibacterial activity of magnesium oxide nanoparticles prepared by Calcination method

2019 ◽  
Vol 10 (03) ◽  
Author(s):  
Elaf Ayad Kadhem ◽  
Miaad Hamzah Zghair ◽  
Sarah , Hussam H. Tizkam, Shoeb Alahmad Salih Mahdi ◽  
Hussam H. Tizkam ◽  
Shoeb Alahmad
Keyword(s):  
Antibacterial Activity ◽  
Magnesium Oxide ◽  
Diffusion Method ◽  
Oxide Nanoparticles ◽  
Gram Negative Bacteria ◽  
Gram Positive ◽  
Gram Negative ◽  
Gram Positive Bacteria ◽  
Magnesium Oxide Nanoparticles ◽  
Agar Disc

magnesium oxide nanoparticles (MgO NPs) were prepared by simple wet chemical method using different calcination temperatures. The prepared NPs were characterized by Electrostatic Discharge (ESD), Scanning Electron Microscope (SEM) and X-ray Diffraction (XRD). It demonstrates sharp intensive peak with the increase of crystallinty and increase of the size with varying morphologies with respect to increase of calcination temperature. Antibacterial studies were done on gram negative bacteria (E.coli) and gram positive bacteria (S.aureus) by agar disc diffusion method. The zones of inhibitions were found larger for gram positive bacteria than gram negative bacteria, this mean, antibacterial MgO NPs activity more active on gram positive bacteria than gram negative bacteria because of the structural differences. It was found that antibacterial activity of MgO NPs was found it has directly proportional with their concentration.

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