Inhibits cell wall synthesis--Ethambutol iv
Bouhss A., Al-Dabbagh B., Vincent M., Odaert B., Aumont-Nicaise M., Bressolier P., Desmadril M., Mengin-Lecreulx D., Urdaci M.C., and Gallay J. 2009. Specific interactions of clausin, a new lantibiotic, with lipid precursors of the bacterial cell wall. , 1390-1397.
-Inhibits synthesis of bacterial cell wall ..
This cell wall, as the antibiotic, contains D-aminoacids, and it has been suggested that an altered metabolism for cell wall synthesis could furnish the precursors for antibiotic synthesis
Bovine tracheal antimicrobial peptide, a cysteine-rich β-defensin produced by respiratory epithelial cells, was active () against the yeast forms of several C. albicans strains. The synthetic form at 400 μg/ml was active against the hyphal forms of A. fumigatus and C. albicans (). In contrast, magainin II, α-defensin, and amphotericin B had lower MICs for A. fumigatus (250, 200, and 0.8 μg/ml, respectively) ().
cells and antagonizing fungal cell wall chitin synthesis
Sova M., Kovač A., Turk S., Hrast M., Blanot D., and Gobec S. 2009. Phosphorylated hydroxyethylamines as novel inhibitors of the bacterial cell wall biosynthesis enzymes MurC to MurF. , 217-222.
an antibiotic acting on the bacterial cell wall, ..
Antifungal peptides are classified by their mode of action. The first group acts by lysis, which occurs via several mechanisms (). Lytic peptides may be amphipathic, that is, molecules with two faces, with one being positively charged and the other being neutral and hydrophobic. Some amphipathic peptides bind only to the membrane surface and can disrupt the membrane structure without traversing the membrane. Others traverse membranes and interact specifically with certain molecules. Finally, other amphipathic peptides aggregate in a selective manner, forming aqueous pores of variable sizes, allowing passage of ions or other solutes. The second peptide group interferes with cell wall synthesis or the biosynthesis of essential cellular components such as glucan or chitin (). An excellent review of lipopeptide antifungal agents affecting cell wall synthesis has been published previously ().
reactions such as cell wall synthesis
Various strains of Bacillus subtilis produce the iturin peptide family. They are small cyclic peptidolipids characterized by a lipid-soluble β-amino acid linked to a peptide containing and amino acids (). Iturins affected membrane surface tension, which caused pore formation and which resulted in the leakage of K+ and other vital ions, paralleling cell death (, , ). One family member, bacillomycin F (Table ), inhibited the growth of fungi including Aspergillus niger, C. albicans, and F. oxysporum (, ). In a disc assay, iturin A inhibited A. flavus and F. moniliforme growth (). Initial clinical trials involving humans and animals showed that iturin A was effective against dermatomycoses and had a wide spectrum of antifungal properties and low allergenic effects (, ). Unfortunately, bacillomycin L and iturin A have been found to be hemolytic, which may reduce their potential use as antifungal drugs ().
term:cubicin = daptomycin (iv) cycline glycopeptide …
The minimum inhibitory concentration (MIC) of an antibiotic is defined as the lowest concentration of the compound that completely inhibits the initiation of growth of a particular bacterium under standardized in vitro conditions. It has been reported that antibiotics at sub-MICs have numerous effects on bacteria, including morphological changes, modifications of cell wall structure, altered growth kinetics, inhibition of enzyme or toxin production, and loss of adhesive properties (). Effects of sub-MICs of antibiotics on bacterial virulence factor expression may provide additional information for the rational use of antimicrobials in clinical practice ().