mbi-226 has been researched along with Bacterial-Infections* in 3 studies
1 review(s) available for mbi-226 and Bacterial-Infections
| Article | Year |
|---|---|
Omiganan pentahydrochloride in the front line of clinical applications of antimicrobial peptides.
Ribosomally synthesized antimicrobial peptides have very wide killing spectra and bacterial resistance to these peptides seems to be a rare phenomenon. Indolicidin is a ribosomally synthesized antimicrobial peptide that served as a template to omiganan, which is in development for the prevention of catheter-related bloodstream infections; clinical trials also proved its efficiency against acne vulgaris. Omiganan is the most advanced molecule in the front line of clinical applications of antimicrobial peptides. The mode and site of action of omiganan are not yet settled although its interaction with membranes is known to play a fundamental role. The biochemical and biophysical foundations for the action of indolicidin and its analogues are reviewed in this paper, as well as the clinical application of omiganan. The in vitro efficiency tests and the outcome of clinical trials are addressed. Altogether, despite the very specific use of omiganan as a topical antibiotic, it has the potential of being a pioneer of a new generation of antibiotics that carry the promise of ending the multi-resistance problem. Topics: Acne Vulgaris; Anti-Infective Agents; Antimicrobial Cationic Peptides; Bacteria; Bacterial Infections; Catheterization; Clinical Trials as Topic; Humans; Patents as Topic | 2006 |
2 other study(ies) available for mbi-226 and Bacterial-Infections
| Article | Year |
|---|---|
Antimicrobial activity of de novo designed cationic peptides against multi-resistant clinical isolates.
Antibiotic resistance is one of the main problems concerning public health or clinical practice. Antimicrobial peptides appear as good candidates for the development of new therapeutic drugs. In this study we de novo designed a group of cationic antimicrobial peptides, analyzed its physicochemical properties, including its structure by circular dichroism and studied its antimicrobial properties against a panel of clinical isolates expressing different mechanisms of resistance. Three cationic alpha helical peptides exhibited antimicrobial activity comparable to, or even better than the comparator omiganan (MBI-226). Topics: Amino Acid Sequence; Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Bacteria; Bacterial Infections; Circular Dichroism; Drug Design; Drug Resistance, Bacterial; Humans; Microbial Sensitivity Tests; Molecular Sequence Data | 2014 |
Omiganan pentahydrochloride (MBI 226), a topical 12-amino-acid cationic peptide: spectrum of antimicrobial activity and measurements of bactericidal activity.
The activity of omiganan pentahydrochloride (formerly MBI 226; a synthetic cationic peptide) was assessed against 1,437 recent clinical bacterial isolates and 214 recent clinical yeast isolates. The omiganan was highly active, and minimal bactericidal concentrations or minimal fungicidal concentrations were either equal to or two- to fourfold higher than MICs. Kill curve experiments showed a clear pattern of bactericidal activity. Topics: Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Bacteria; Bacterial Infections; Candida; Candidiasis; Colony Count, Microbial; Drug Stability; Freezing; Humans; Kinetics; Microbial Sensitivity Tests; Oxacillin; Penicillin Resistance; Penicillins; Vancomycin Resistance | 2004 |