Antimicrobial properties of N3-(iodoacetyl)-L-2,3-diaminopropanoic acid-peptide conjugates
| Autor: | Teresa Zieniawa, Henryk Chmara, Ryszard Andruszkiewicz, Edward Borowski, Sławomir Milewski |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Antifungal Agents
Stereochemistry Lysine Glucose-6-Phosphate Peptide Peptidoglycan chemistry.chemical_compound Structure-Activity Relationship Glucosamine Cell Wall Drug Discovery Candida albicans Antibacterial agent chemistry.chemical_classification Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) Dipeptide biology Bacillus pumilus Chemistry Glucosephosphates Biological Transport biology.organism_classification Antimicrobial Anti-Bacterial Agents Biochemistry beta-Alanine Molecular Medicine Norvaline Bacillus subtilis |
| Zdroj: | Journal of medicinal chemistry. 33(10) |
| ISSN: | 0022-2623 |
| Popis: | Six peptide conjugates consisting of either norvaline, methionine, or lysine and N3-(iodoacetyl)-L-2,3-diaminopropanoic acid--a strong, irreversible inactivator of bacterial and fungal glucosamine-6-phosphate synthase--were synthesized and their antibacterial and antifungal activities were evaluated. Antimicrobial potencies of these peptides were correlated with their transport and cleavage rates inside the cells. Bacteriolysis of Bacillus pumilus cells and inhibition of [14C]glucose incorporation into cell-wall polysaccharides of Candida albicans as a result of glucosamine 6-phosphate inactivation were also observed. Reversal of growth inhibitory effect of these peptides by N-acetylglucosamine in bacteria and fungi suggests the effective delivery of N3-iodoacetyl-L-2,3-diaminopropanoic acid into the cell by a peptide-transport system. |
| Databáze: | OpenAIRE |
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