Effects of single amino acid substitutions on peptide interaction with lipid membranes and bacteria-variants of GKE21, an internal sequence from human LL-37

Colloids and Surfaces A: Physicochemical and Engineering Aspects

Volumn 354, Issue 1-3, 2010, Pages 65-71

  Ringstad, Lovisa ^a   Schmidtchen, Artur ^b   Malmsten, Martin ^a  

^a UPPSALA UNIVERSITY   (Sweden)

^b LUND UNIVERSITY   (Sweden)

Author keywords

AMP; Antimicrobial peptide; Ellipsometry; Liposome; LL 37

Indexed keywords

ADSORPTION; AMINO ACIDS; BACTERIOLOGY; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; DRUG INTERACTIONS; ELLIPSOMETRY; FLUORESCENCE SPECTROSCOPY; ORGANIC ACIDS; PHOSPHOLIPIDS; POLYPEPTIDES;

AMINO ACID SUBSTITUTION; AMP; AMPHIPHILICITY; ANTIMICROBIAL PEPTIDE; BACTERIAL KILLING; BACTERICIDAL PROPERTIES; CATHELICIDIN; CIRCULAR DICHROISM; D-VALINE; ELECTROLYTE CONCENTRATION; ELECTROSTATIC INTERACTIONS; HELIX FORMATION; ISO-ELECTRIC POINTS; LIPID MEMBRANES; NET CHARGES; PEPTIDE ADSORPTION; PHOSPHOLIPID MEMBRANE; RADIAL DIFFUSION;

PEPTIDES;

AMPHOPHILE; ANTIMICROBIAL PEPTIDE GKE21; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; ISOLEUCINE; LIPOSOME; PHENYLALANINE; POLYPEPTIDE ANTIBIOTIC AGENT; PROLINE; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE;

ADSORPTION; AMINO ACID SUBSTITUTION; ARTICLE; BACTERICIDAL ACTIVITY; CIRCULAR DICHROISM; CONTROLLED STUDY; ELLIPSOMETRY; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; IMMUNODIFFUSION; LIPID BILAYER; LIPOPHILICITY; MEMBRANE BINDING; PH; PHOSPHOLIPID MEMBRANE; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; SUBSTITUTION REACTION;

EID: 73049084108     PISSN: 09277757     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.colsurfa.2009.04.018     Document Type: Article

References (34)

1. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
2. Marr A.K., Gooderham W.J., and Hancock R.E.W. Antibacterial peptides for therapeutic use: obstacles and realistic outlook. Curr. Opin. Pharmacol. 6 (2006) 1-5
3. Toke O. Antimicrobial peptides: new candidates in the fight against bacterial infections. Biopolymers 80 (2005) 717-735
4. Nizet V. Antimicrobial peptide resistance mechanisms of human bacterial pathogens. Curr. Issues Mol. Biol. 8 (2006) 11-26
5. Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Microbiol. 3 (2005) 238-250
6. Huang H.W. Molecular mechanism of antimicrobial peptides: the origin of cooperativity. Biochim. Biophys. Acta 1758 (2006) 1292-1302
7. Hancock R.E., and Sahl H.G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24 (2006) 1551-1557
8. Ringstad L., Schmidtchen A., and Malmsten M. Effect of peptide length on the interaction between consensus peptides and DOPC/DOPA bilayers. Langmuir 22 (2006) 5042-5050
9. Ringstad L., Kacprzyk L., Schmidtchen A., and Malmsten M. Effects of topology, length, and charge on the activity of a kininogen-derived peptide on lipid membranes and bacteria. Biochim. Biophys. Acta 1768 (2007) 715-727
10. Tossi A., Sandri L., and Giangaspero A. Amphipatic, α-helical antimicrobial peptides. Biopolymers 55 (2000) 4-30
11. A. Schmidtchen, M. Pasipuleti, M. Mörgelin, M. Malmsten, Tagging of antimicrobial peptides by hydrophobic amino acids-a facile approach for enhancing membrane incorporation and bacterial killing, J. Biol. Chem. (2008), in press.
12. Ringstad L., Andersson Nordahl E., Schmidtchen A., and Malmsten M. Composition effect on peptide interaction with lipids and bacteria: variants of C3a peptide CNY21. Biophys. J. 92 (2007) 87-98
13. Ringstad L., Protopapa E., Lindholm-Sethson B., Schmidtchen A., Nelson A., and Malmsten M. An electrochemical study into the interaction between complement-derived peptides and DOPC mono- and bilayers. Langmuir 24 (2008) 208-216
14. Bechinger B. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta 1462 (1999) 157-183
15. Chen F.-Y., Lee M.-T., and Huang H.W. Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation. Biophys. J. 84 (2003) 3751-3758
16. Strömstedt A.A., Pasupuleti M., Schmidtchen A., and Malmsten M. Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37. Antimicrob. Agents Chemother. 53 (2009) 593-602
17. In: Simon S.A., and McIntosh T.J. (Eds). Peptide-Lipid Interactions (2002), Academic Press, New York
18. Malmsten M., Burns N., and Veide A. Electrostatic and hydrophobic effects of oligopeptide insertions on protein adsorption. J. Colloid Interface Sci. 204 (1998) 104-111
19. Lehrer R.I., Rosenman M., Harwig S.S., Jackson R., and Eisenhauer P. Ultrasensitive assays for endogenous antimicrobial polypeptides. J. Immunol. Methods 137 (1991) 167-173
20. Andersson E., Rydengard V., Sonesson A., Morgelin M., Bjorck L., and Schmidtchen A. Antimicrobial activities of heparin-binding peptides. Eur. J. Biochem. 271 (2004) 1219-1226
21. Greenfield N., and Fasman G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8 (1969) 4108-4116
22. Sjogren H., and Ulvenlund S. Comparison of the helix-coil transition of a titrating polypeptide in aqueous solutions and at the air-water interface. Biophys. Chem. 116 (2005) 11-21
23. De Feijter J.A., Benjamins J., and Veer F.A. Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air-water interface. Biopolymers 17 (1978) 1759-1772
24. Tiberg F., Harwigsson I., and Malmsten M. Formation of model lipid bilayers at the silica-water interface by co-adsorption with non-ionic dodecyl maltoside surfactant. Eur. Biophys. J. 29 (2000) 196-203
25. Durr U.H., Sudheendra U.S., and Ramamoorthy A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim. Biophys. Acta 1758 (2006) 1408-1425
26. Schmidtchen A., Frick I.-M., Andersson E., Tapper H., and Björck L. Proteinases of common pathogenic bacteria degrade and inactivate the antibacterial peptide LL-37. Mol. Microbiol. 46 (2002) 157-168
27. Murakami M., Lopez-Garcia B., Braff M., Dorschner R.A., and Gallo R.L. Postsecretoty processing generates multiple cathelicidins for enhanced topical antimicrobial defense. J. Immunol. 172 (2004) 3070-3077
28. Sieprawska-Lupa M., Mydel P., Krawczyk K., Wojcik K., Puklo M., Lupa B., Suder P., Silberring J., Reed M., Pohl J., Shafer W., McAleese F., Foster T., Travis J., and Potempa J. Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureus-derived proteinases. Antimicrob. Agents Chemother. 48 (2004) 4673-4679
29. Braff M.H., Hawkins M.A., Di Nardo A., Lopez-Garcia B., Howell M.D., Wong C., Lin K., Streib J.E., Dorschner R., Leung D.Y.M., and Gallo R.L. Structure-function relationships among human cathelicidin peptides: dissociation of antimicrobial properties from host immunostimulatory activities. J. Immunol. 174 (2005) 4271-4278
30. Nagaoka I., Hirota S., Niyonsaba F., Hirata M., Adachi Y., Tamura H., Tanaka S., and Heumann D. Augmentation of the lipopolysaccharide-neutralizing activities of human cathelicidin CAP18/LL-37-derived antimicrobial peptides by replacement with hydrophobic and cationic amino acid residues. Clin. Diag. Lab. Immunol. 9 (2002) 972-982
31. Nell M.J., Tjabringa G.A., Wafelman A.R., Verrijk R., Hiemstra P.S., Drijfhout J.W., and Grote J.J. Development of novel LL-37 derived antimicrobial peptides with LPS and LTA neutralizing and antimicrobial activities for therapeutic application. Peptides 27 (2006) 649-660
32. Li X., Li Y., Han H., Miller D.W., and Wang G. Solution structures of human LL-37 fragments and NMR-based identification of minimal membrane-targeting antimicrobial anticancer region. J. Am. Chem. Soc. 128 (2006) 5776-5785
33. Wang G., Watson K.M., and Buckheit R.W. Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. Antimicrob. Agents Chemother. 52 (2008) 3438-3440
34. Sigurdadottir T., Andersson P., Davoudi M., Malmsten M., Schmidtchen A., and Bodelsson M. In silico identification and biological evaluation of antimicrobial peptides based on human cathelicidin LL-37. Antimicrob. Agents. Chemother. 50 (2006) 2983-2989