Novel antimicrobial peptides with high anticancer activity and selectivity.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 25970292.
- Also identified by DOI 10.1371/journal.pone.0126390 and PMC identifier 4430538.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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 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 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.
Medical subject headings
- Anti-Bacterial Agents
- Antibiotics, Antineoplastic
- Antimicrobial Cationic Peptides
- Lung Neoplasms