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Novel antimicrobial peptides with high anticancer activity and selectivity.

Chu HL, Yip BS, Chen KH, Yu HY, Chih YH, Cheng HT, Chou YT, Cheng JW - PLoS ONE (2015)

Bottom Line: 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.Fluorescence microscopic studies indicated that the FITC-labeled K4R2-Nal2-S1 preferentially binds cancer cells and causes apoptotic cell death.Our strategy provides new opportunities in the development of highly effective and selective antimicrobial and anticancer peptide-based therapeutics.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biotechnology and Department of Medical Science, National Tsing Hua University, Hsinchu, 300, Taiwan.

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.

No MeSH data available.


Related in: MedlinePlus

Plots of the activities of S1, Nal2-S1, K4R2-Nal2-S1, and K6-Nal2-S1 against OECM-1, C9, SAS, A549, PC9, PC9-G cancer cell lines.
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pone.0126390.g002: Plots of the activities of S1, Nal2-S1, K4R2-Nal2-S1, and K6-Nal2-S1 against OECM-1, C9, SAS, A549, PC9, PC9-G cancer cell lines.

Mentions: The cytotoxicities of S1 and its analogs on human lung cancer cells (i.e, PC9, PC9-G and A549), human oral cancer cells (i.e, C9, OECM-1, and SAS), and human fibroblast (HFW) were evaluated by MTT assay for 24 hours. The data showed that the three Nal-embedded peptides all have potent anticancer activities against different cancer cell lines (Fig 2). Similar results were observed at earlier time points (i.e. 3 hours and 12 hours) (S1 and S2 Figs).


Novel antimicrobial peptides with high anticancer activity and selectivity.

Chu HL, Yip BS, Chen KH, Yu HY, Chih YH, Cheng HT, Chou YT, Cheng JW - PLoS ONE (2015)

Plots of the activities of S1, Nal2-S1, K4R2-Nal2-S1, and K6-Nal2-S1 against OECM-1, C9, SAS, A549, PC9, PC9-G cancer cell lines.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4430538&req=5

pone.0126390.g002: Plots of the activities of S1, Nal2-S1, K4R2-Nal2-S1, and K6-Nal2-S1 against OECM-1, C9, SAS, A549, PC9, PC9-G cancer cell lines.
Mentions: The cytotoxicities of S1 and its analogs on human lung cancer cells (i.e, PC9, PC9-G and A549), human oral cancer cells (i.e, C9, OECM-1, and SAS), and human fibroblast (HFW) were evaluated by MTT assay for 24 hours. The data showed that the three Nal-embedded peptides all have potent anticancer activities against different cancer cell lines (Fig 2). Similar results were observed at earlier time points (i.e. 3 hours and 12 hours) (S1 and S2 Figs).

Bottom Line: 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.Fluorescence microscopic studies indicated that the FITC-labeled K4R2-Nal2-S1 preferentially binds cancer cells and causes apoptotic cell death.Our strategy provides new opportunities in the development of highly effective and selective antimicrobial and anticancer peptide-based therapeutics.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biotechnology and Department of Medical Science, National Tsing Hua University, Hsinchu, 300, Taiwan.

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.

No MeSH data available.


Related in: MedlinePlus