Rational design of anti-microbial peptides with enhanced activity and low cytotoxicity based on the structure of the arginine/histidine-rich peptide, chensinin-1

Journal of Applied Microbiology

Volumn 113, Issue 3, 2012, Pages 677-685

  Shang, D ^a,b   Sun, Y ^a   Wang, C ^b   Ma, L ^b   Li, J ^a   Wang, X ^b  

^a LIAONING NORMAL UNIVERSITY   (China)

^b Liaoning Provincial Key Laboratory of Biotechnology and Drug Discovery   (China)

Author keywords

Amphipathicity; Anti microbial peptide; Calcein loaded liposomes; Chensinin 1; Helicity; Hydrophobicity

Indexed keywords

AMINO ACIDS; BACTERIA; CELL MEMBRANES; CIRCULAR DICHROISM SPECTROSCOPY; CONFORMATIONS; DICHROISM; ETHANOL; HYDROPHOBICITY; LIPOSOMES; SODIUM COMPOUNDS; SULFUR COMPOUNDS;

AMPHIPATHICITY; ANTIMICROBIAL PEPTIDE; CALCEIN; CALCEIN-LOADED LIPOSOME; CHENSININ-1; HELICITIES; LOW CYTOTOXICITIES; RATIONAL DESIGN; STRUCTURE-ACTIVITY RELATIONSHIPS; THERAPEUTIC AGENTS;

PEPTIDES;

CHENSININ 1 DERIVATIVE; GLYCINE; LEUCINE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

ANTIMICROBIAL ACTIVITY; BACTERIUM; BIOTECHNOLOGY; CHEMICAL REACTION; CYTOLOGY; DISEASE TREATMENT; DRUG DEVELOPMENT; HYDROPHOBICITY; LIPID; MEMBRANE; PEPTIDE; SPECTROSCOPY; TOXICOLOGY;

ACINETOBACTER BAUMANNII; AMINO ACID SUBSTITUTION; ANTIMICROBIAL ACTIVITY; ARTICLE; BACILLUS CEREUS; BACTERICIDAL ACTIVITY; CELL PERMEABILIZATION; CIRCULAR DICHROISM; CONTROLLED STUDY; CYTOTOXICITY; DRUG SYNTHESIS; ENTEROBACTER AEROGENES; ENTEROBACTER CLOACAE; ENTEROCOCCUS FAECALIS; ENTEROCOCCUS FAECIUM; ESCHERICHIA COLI; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; HEMOLYSIS; HUMAN; HUMAN CELL; HUMAN TISSUE; HYDROPHILICITY; HYDROPHOBICITY; KLEBSIELLA PNEUMONIAE; LACTOCOCCUS LACTIS; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PROTEIN CONFORMATION; PROTEUS MIRABILIS; PSEUDOMONAS AERUGINOSA; STAPHYLOCOCCUS AUREUS; STRUCTURE ACTIVITY RELATION;

POSIBACTERIA;

EID: 84865297339     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/j.1365-2672.2012.05355.x     Document Type: Article

References (33)

1. Carver, T. and Bleasby, A. (2003) The design of Jemboss: a graphical user interface to EMBOSS. Bioinformatics 19, 1837-1843.
2. Chen, Y., Mant, C.T., Farmer, S.W., Hancock, R.W., Vasilp, M.L. and Hodges, R.S. (2005) Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J Biol Chem 280, 12316-12329.
3. Chen, Y., Guarnieri, M.T., Vasil, A.I., Vasil, M.L., Mant, C.T. and Hodges, R.S. (2007a) Role of peptide hydrophobicity in the mechanism of action of α-helical antimicrobial peptides. Antimicrob Agents Chemother 51, 1398-1406.
4. Chen, Y., Mant, C.T. and Hodges, R.S. (2007b) Preparative reversed-phase high-performance liquid chromatography collection efficiency for an antimicrobial peptide on columns of varying diameters (1mm to 9·4mm I.D.). J Chromatogr A 1140, 112-120.
5. Chi, S.W., Kim, J.S., Kim, D.H., Lee, S.H., Park, Y.H. and Han, K.H. (2007) Solution structure and membrane interaction mode of an antimicrobial peptide gaegurin 4. Biochem Biophy Res Commun 352, 592-597.
6. Chou, H.T., Kuo, T.Y. and Chiang, J.C. (2008) Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. Int J Antimicrob Agents 32, 130-138.
7. Coccia, C., Rinaldi, A.C., Luca, V., Barra, D., Bozzi, A., Giulio, A.D., Veerman, E.C. and Mangoni, M.L. (2011) Membrane interaction and antibacterial properties of two mildly cationic peptide diastereomers, bombinins H2 and H4, isolated from Bombina skin. Eur Biophys J 40, 577-588.
8. Conlon, J.M., Kolodziejek, J. and Nowotny, N. (2004) Antimicrobial peptides from ranidae frogs: taxonomic and phylogenetic markers and a potential source of new therapeutic agents. Biochim Biophys Acta 1696, 1-14.
9. Conlon, J.M., Ahmed, E. and Condamine, E. (2009) Antimicrobial properties of brevinin-2-related peptide and its analogs: efficacy against multidrug-resistant Acinetobacter baumannii. Chem Biol Drug Des 74, 488-493.
10. Dathe, M., Wieprecht, T., Nikolenko, H., Handel, L., Maloy, W.L., MacDonald, D.L., Beyermann, M. and Bienert, M. (1997) Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Lett 403, 208-212.
11. Eisenberg, D., Weiss, R.M. and Terwilliger, T.C. (1982) The helical hydrophobic moment: a measure of the amphiphilicity of a helix. Nature 299, 371-374.
12. Epand, R.F., Schmitt, M.A., Gellman, S.H. and Epand, R.M. (2006) Role of membrane lipids in the mechanism of bacterial species selective toxicity by two α/β-antimicrobial peptides. Biochim Biophys Acta 1758, 1343-1350.
13. Giangaspero, A., Sandri, L. and Tossi, A. (2001) Amphipathic α-helical peptides. A systematic study of the effects of structural and physical properties on biological activity. Eur J Biochem 268, 5589-5600.
14. Ishibashi, J., Sakanaka, H.S., Yang, J., Sagisaka, A. and Yamakawa, M. (1999) Purification, cDNA cloning and modification of a defensin from the coconut rhinoceros beetle, Oryctes rhinoceros. Eur J Biochem 266, 616-623.
15. Jiang, Z., Vasil, A.I., Hale, J.D., Hancock, R.E.W., Vasil, M.L. and Hodges, R.S. (2007) Effects of net charge and the number of positively charged residues on the biological activity of amphipathic α-helical cationic antimicrobial peptides. Biopolymers 90, 369-383.
16. Jiang, Z., Vasil, A.I. and Gera, L. (2011) Rational design of α-helical antimicrobial peptides to target gram-negative pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: utilization of charge, specificity determinants, total hydrophobicity, hydrophobe type and location as design parameters to improve the therapeutic ratio. Chem Biol Drug Des 77, 225-240.
17. Kan, E.J., Demel, R.A., Bent, A. and Kruijff, B. (2003) The role of the abundant phenylalanines in the mode of action of the antimicrobial peptide clavanin. Biochim Biophys Acta 1615, 84-92.
18. Leptihn, S., Har, J.Y., Wohland, T. and Ding, J.L. (2010) Correlation of charge, hydrophobicity, and structure with antimicrobial activity of s1 and MIRIAM peptides. Biochemistry 49, 9161-9170.
19. Lequin, O., Ladram, A. and Chabbert, L. (2006) Dermaseptin S9, An α-helical antimicrobial peptide with a hydrophobic core and cationic termini. Biochemistry 45, 468-480.
20. Li, L., He, J., Eckert, R., Yarbrough, D., Lux, R., Anderson, M. and Shi, W. (2010) Design and characterization of an acid-activated antimicrobial peptide. Chem Biol Drug Des 75, 127-132.
21. Mant, C.T., Kovacs, J.M., Kim, H.M., Kim, H.M., Pollock, D.D. and Hodges, R.S. (2009) Intrinsic amino acid side-chain hydrophilicity/hydrophobicity coefficients determined by reversed-phase high-performance liquid chromatography of model peptides: comparison with other hydrophilicity/hydrophobicity scales. Biopolymers 92, 573-595.
22. Matsuzaki, K., Murase, O., Fujii, N. and Miyajima, K. (1996) An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry 35, 11361-11368.
23. Pàl, T., Sonnevend, A., Galadari, S. and Conlon, J.M. (2005) Design of potent, non-toxic antimicrobial agents based upon the structure of the frog skin peptide, pseudin-2. Regul Pept 129, 85-91.
24. Papo, N. and Shai, Y. (2005) A molecular mechanism for lipopolysaccharide protection of gram-negative bacteria from antimicrobial peptides. J Biol Chem 280, 10378-10387.
25. Rasul, R., Colea, N., Balasubramanian, D., Chen, R., Kumar, N. and Willcox, M.D.P. (2010) Interaction of the antimicrobial peptide melimine with bacterial membranes. Int J Antimicrob Agents 35, 566-572.
26. Rozek, A., Friedrich, C.L. and Hancock, R.E.W. (2000) Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry 39, 15765-15774.
27. Sansom, M.S. (1991) The biophysics of peptide models of ion channels. Prog Biophys Mol Biol 55, 139-235.
28. Shai, Y. (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim Biophys Acta 1462, 55-70.
29. Shang, D.J., Yu, F., Li, J., Zheng, J., Zhang, L. and Li, Y. (2009) Molecular cloning of cDNAs encoding antimicrobial peptide precursors from the skin of the Chinese brown frog, Rana chensinensis. Zool Sci 26, 220-226.
30. Shang, D.J., Sun, Y., Wang, C., Wei, S., Ma, L.J. and Sun, L. (2012) Membrane interaction and antibacterial properties of chensinin-1, an antimicrobial peptide with atypical structural features from the skin of Rana chensinensis. Appl Microbiol Biotechnol, in press. doi: 10.1007/s00253-012-4148-3.
31. Szabo, D., Ostorhazi, E., Binas, A., Rozgonyi, F., Kocsis, B., Cassone, M., Wade, J.D., Nolte, O. et al. (2010) The designer proline-rich antibacterial peptide A3-APO is effective against systemic Escherichia coli infections in different mouse models. Int J Antimicrob Agents 35, 357-361.
32. Wieprecht, T., Dathe, M., Krause, E., Beyermann, M., Maloy, W.L., MacDonald, D.L. and Bienert, M. (1997) Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment. FEBS Lett 417, 135-140.
33. Yeaman, M.R. and Yount, N.Y. (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55, 27-55.