Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance

Antimicrobial peptides (AMPs) have been recognised as a significant therapeutic option for mitigating resistant microbial infections. It has been found recently that Plasmodium falciparum-derived, 20 residue long, peptide 35409 had antibacterial and haemolytic activity, making it an AMP having reduc...

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Bibliographic Details
Published in:Microorganisms (Basel) 2020-06, Vol.8 (6), p.867
Main Authors: Barreto-Santamaría, Adriana, Rivera, Zuly Jenny, García, Javier Eduardo, Curtidor, Hernando, Patarroyo, Manuel Elkin, Patarroyo, Manuel Alfonso, Arévalo-Pinzón, Gabriela
Format: Article
Language:English
Subjects:
Amino acids
Antibiotics
Antimicrobial agents
antimicrobial peptide
Antimicrobial peptides
Bacteria
Bacterial infections
Bioinformatics
Biological activity
Chemical synthesis
Chromatography
Clinical isolates
Clinical trials
E coli
Escherichia coli
FDA approval
Health aspects
Membranes
Microorganisms
minimum bactericidal concentration (MBC)
minimum haemolytic concentration (MHC)
minimum inhibitory concentration (MIC)
Mucositis
Nosocomial infections
Peptides
Residues
Selectivity
Solvents
Synthetic peptides
therapeutic index (TI)
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Summary:Antimicrobial peptides (AMPs) have been recognised as a significant therapeutic option for mitigating resistant microbial infections. It has been found recently that Plasmodium falciparum-derived, 20 residue long, peptide 35409 had antibacterial and haemolytic activity, making it an AMP having reduced selectivity, and suggesting that it should be studied more extensively for obtaining new AMPs having activity solely targeting the bacterial membrane. Peptide 35409 was thus used as template for producing short synthetic peptides (
ISSN:2076-2607
2076-2607
DOI:10.3390/microorganisms8060867