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Novel antimicrobial peptides with high anticancer activity and selectivity.

ABSTRACT: We describe a strategy to boost anticancer activity and reduce normal cell toxicity of short antimicrobial peptides by adding positive charge amino acids and non-nature bulky amino acid ?-naphthylalanine residues to their termini. Among the designed peptides, K4R2-Nal2-S1 displayed better salt resistance and less toxicity to hRBCs and human fibroblast than Nal2-S1 and K6-Nal2-S1. Fluorescence microscopic studies indicated that the FITC-labeled K4R2-Nal2-S1 preferentially binds cancer cells and causes apoptotic cell death. Moreover, a significant inhibition in human lung tumor growth was observed in the xenograft mice treated with K4R2-Nal2-S1. Our strategy provides new opportunities in the development of highly effective and selective antimicrobial and anticancer peptide-based therapeutics.

SUBMITTER: Chu HL

PROVIDER: S-EPMC4430538 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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Novel antimicrobial peptides with high anticancer activity and selectivity.

Chu Hung-Lun HL Yip Bak-Sau BS Chen Kuan-Hao KH Yu Hui-Yuan HY Chih Ya-Han YH Cheng Hsi-Tsung HT Chou Yu-Ting YT Cheng Jya-Wei JW

PloS one 20150513 5

We describe a strategy to boost anticancer activity and reduce normal cell toxicity of short antimicrobial peptides by adding positive charge amino acids and non-nature bulky amino acid β-naphthylalanine residues to their termini. Among the designed peptides, K4R2-Nal2-S1 displayed better salt resistance and less toxicity to hRBCs and human fibroblast than Nal2-S1 and K6-Nal2-S1. Fluorescence microscopic studies indicated that the FITC-labeled K4R2-Nal2-S1 preferentially binds cancer cells and c ...[more]

PMID: 25970292

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