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Int J Microbiol. 2012;2012:764834. doi: 10.1155/2012/764834. Epub 2012 Feb 16.

The Design and Construction of K11: A Novel α-Helical Antimicrobial Peptide.

International journal of microbiology

Huang Jin-Jiang, Lu Jin-Chun, Lu Min, Huang Qing-Shan, Li Guo-Dong

Affiliations

  1. State Key Laboratory of Genetic Engineering, Institute of Genetics, College of Life Science, Fudan University, Shanghai 200433, China.

PMID: 22518150 PMCID: PMC3299254 DOI: 10.1155/2012/764834

Abstract

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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