Publication | Open Access
The Design and Construction of K11: A Novel<i>α</i>-Helical Antimicrobial Peptide
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Citations
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References
2012
Year
Peptide EngineeringKlebsiella PneumoniaeAntimicrobial PeptidesPeptide SciencePeptide TherapeuticsPeptide ChemistryAntimicrobial ChemotherapyBacterial PathogensDrug ResistanceDerivative Peptide K11Tested PeptidesAntimicrobial ResistanceHealth SciencesAntimicrobial Drug DiscoveryBiochemistryAntibacterial AgentAntimicrobial CompoundPharmacologyMolecular ModelingClinical MicrobiologyAntimicrobial SusceptibilityAntibioticsPeptide TherapeuticPeptide SynthesisMicrobiologyAntimicrobial PharmacodynamicsMedicine
Amphipathic α-helical antimicrobial peptides comprise a class of broad-spectrum agents that are used against pathogens. We designed a series of antimicrobial peptides, CP-P (KWKSFIKKLTSKFLHLAKKF) and its derivatives, and determined their minimum inhibitory concentrations (MICs) against Pseudomonas aeruginosa, their minimum hemolytic concentrations (MHCs) for human erythrocytes, and the Therapeutic Index (MHC/MIC ratio). We selected the derivative peptide K11, which had the highest therapeutic index (320) among the tested peptides, to determine the MICs against Gram-positive and Gram-negative bacteria and 22 clinical isolates including Acinetobacter baumannii, methicillin-resistant Staphylococcus aureus, Pseudomonas aeruginosa, Staphylococcus epidermidis, and Klebsiella pneumonia. K11 exhibited low MICs (less than 10 μg/mL) and broad-spectrum antimicrobial activity, especially against clinically isolated drug-resistant pathogens. Therefore, these results indicate that K11 is a promising candidate antimicrobial peptide for further studies.
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