Antibacterial Activity of a Cationic Antimicrobial Peptide against Multidrug-Resistant Gram-Negative Clinical Isolates and Their Potential Molecular Targets

Autor: Jose Oñate-Garzón, Dorian Polo-Cerón, Iván Darío Ocampo-Ibáñez, Paola Andrea Londoño, Alberto Aragón-Muriel, Adriana Correa, Liliana Janeth Flórez-Elvira, Juan David Londoño-Mosquera, Sandra Patricia Rivera-Sánchez, Helen Astrid Agudelo-Góngora
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Klebsiella pneumoniae
Pharmaceutical Science
multidrug-resistant Klebsiella pneumoniae
medicine.disease_cause
Article
Analytical Chemistry
Microbiology
lcsh:QD241-441
03 medical and health sciences
Minimum inhibitory concentration
lcsh:Organic chemistry
Drug Resistance
Multiple
Bacterial

Drug Discovery
medicine
Humans
Physical and Theoretical Chemistry
Protein Precursors
cationic antimicrobial peptide
030304 developmental biology
0303 health sciences
biology
030306 microbiology
Pseudomonas aeruginosa
Chemistry
Organic Chemistry
Broth microdilution
biology.organism_classification
Antimicrobial
multidrug-resistant Pseudomonas aeruginosa
Anti-Bacterial Agents
Multiple drug resistance
Cecropin
Chemistry (miscellaneous)
Molecular Medicine
Insect Proteins
Antibacterial activity
Antimicrobial Cationic Peptides
Zdroj: Molecules
Volume 25
Issue 21
Molecules, Vol 25, Iss 5035, p 5035 (2020)
ISSN: 1420-3049
Popis: Antimicrobial resistance reduces the efficacy of antibiotics. Infections caused by multidrug-resistant (MDR), Gram-negative bacterial strains, such as Klebsiella pneumoniae (MDRKp) and Pseudomonas aeruginosa (MDRPa), are a serious threat to global health. However, cationic antimicrobial peptides (CAMPs) are promising as an alternative therapeutic strategy against MDR strains. In this study, the inhibitory activity of a cationic peptide, derived from cecropin D-like (&Delta
M2), against MDRKp and MDRPa clinical isolates, and its interaction with membrane models and bacterial genomic DNA were evaluated. In vitro antibacterial activity was determined using the broth microdilution test, whereas interactions with lipids and DNA were studied by differential scanning calorimetry and electronic absorption, respectively. A strong bactericidal effect of &Delta
M2 against MDR strains, with minimal inhibitory concentration (MIC) and minimal bactericidal concentrations (MBC) between 4 and 16 &mu
g/mL, was observed. The peptide had a pronounced effect on the thermotropic behavior of the 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)/1,2-dimyristoyl-sn-glycero-3-phosphorylglycerol (DMPG) membrane models that mimic bacterial membranes. Finally, the interaction between the peptide and genomic DNA (gDNA) showed a hyperchromic effect, which indicates that &Delta
M2 can denature bacterial DNA strands via the grooves.
Databáze: OpenAIRE
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