Candidacidal mechanism of a Leu/Lys-rich α-helical amphipathic model antimicrobial peptide and its diastereomer composed of D,L-amino acids

Journal of Peptide Science

Volumn 16, Issue 11, 2010, Pages 601-606

  Wang, Peng ^a   Nan, Yong Hai ^a   Shin, Song Yub ^a,b  

^a Chosun University   (South Korea)

^b Chosun University College of Medicine   (South Korea)

Author keywords

Candidacidal activity; Candidacidal mechanism; Diastereomeric peptide; Leu Lys rich helical model antimicrobial peptide

Indexed keywords

ANTIINFECTIVE AGENT; BETAINE; CALCEIN; DEXTRO AMINO ACID; ERGOSTEROL; FLUORESCEIN ISOTHIOCYANATE; LEUCINE; POLYPEPTIDE ANTIBIOTIC AGENT;

ALPHA HELIX; ANIMAL CELL; ANTIFUNGAL ACTIVITY; ARTICLE; CANDIDA ALBICANS; CELL MEMBRANE; CELL SELECTION; CELL WALL; CHANNEL GATING; CONFOCAL LASER MICROSCOPY; CONTROLLED STUDY; DIASTEREOISOMER; DRUG MECHANISM; FLUORESCENCE SPECTROSCOPY; FUNGAL CELL; HEMOLYSIS; HUMAN; HUMAN CELL; NONHUMAN; ORGANISMAL INTERACTION; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANTIFUNGAL AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CANDIDA ALBICANS; CELL MEMBRANE; MOLECULAR SEQUENCE DATA; PHOSPHOLIPIDS; PROTEIN STRUCTURE, SECONDARY; STEREOISOMERISM;

CANDIDA; CANDIDA ALBICANS;

EID: 78650428458     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1268     Document Type: Article

References (34)

1. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-395.
2. Hancock RE, Scott MG. The role of antimicrobial peptides in animal defenses. Proc. Nat. Acad. Sci. U.S.A. 2000; 97: 8856-8861.
3. Hancock RE, Diamond G. The role of cationic antimicrobial peptides in innate host defences. Trends Microbiol. 2000; 8: 402-410.
4. Andreu D, Rivas L. Animal antimicrobial peptides: an overview. Biopolymers 1998; 47: 415-433.
5. Tossi A, Sandri L, Giangaspero A. Amphipathic, α-helical antimicrobial peptides. Biopolymers 2000; 55: 4-30.
6. Helmerhorst EJ, Reijnders IM, Van't Hof W, Veerman EC, Nieuw AV. A critical comparison of the hemolytic and fungicidal activities of cationic antimicrobial peptides. FEBS Lett. 1999; 449: 105-110.
7. Oren Z, Shai Y. Cyclization of a cytolytic amphipathic α-helical peptide and its diastereomer: effect on structure, interaction with model membranes, and biological function. Biochemistry 2000; 39: 6103-6114.
8. Dathe M, Meyer J, Beyermann M, Maul B, Hoischen C, Bienert M. General aspects of peptide selectivity towards lipid bilayers and cell membranes studied by variation of the structural parameters of amphipathic helical model peptides. Biochim. Biophys. Acta 2002; 1558: 171-186.
9. Song YM, Yang ST, Lim SS, Kim Y, Hahm KS, Kim JI, Shin SY. Effects of L- or D-Pro incorporation into hydrophobic or hydrophilic helix face of amphipathic α-helical model peptide on structure and cell selectivity. Biochem. Biophys. Res. Commun. 2004; 314: 615-621.
10. Zhu WL, Song YM, Park Y, Park KH, Yang ST, Kim JI, Park IS, Hahm KS, Shin SY. Substitution of the leucine zipper sequence in melittin with peptoid residues affects self-association, cell selectivity, and mode of action. Biochim. Biophys. Acta 2007; 1768: 1506-1517.
11. Matsuzaki K. Control of cell selectivity of antimicrobial peptides. Biochim. Biophys. Acta 2009; 1788: 1687-1692.
12. Shai Y, Oren Z. Diastereoisomers of cytolysins, a novel class of potent antibacterial peptides. J. Biol. Chem. 1996; 271: 7305-7308.
13. Oren Z, Shai Y. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry 1997; 36: 1826-1835.
14. Oren Z, Hong J, Shai Y. A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity. J. Biol. Chem. 1997; 272: 14643-14649.
15. Sharon M, Oren Z, Shai Y. Anglister J. 2D-NMR and ATR-FTIR study of the structure of a cell-selective diastereomer of melittin and its orientation in phospholipids. Biochemistry 1999; 38: 15305-15316.
16. Hong J, Oren Z, Shai Y. Structure and organization of hemolytic and nonhemolytic diastereomers of antimicrobial peptides in membranes. Biochemistry 1999; 38: 16963-16973.
17. Papo N, Oren Z, Pag U, Sahl HG, Shai Y. The consequence of sequence alteration of an amphipathic α-helical antimicrobial peptide and its diastereomers. J. Biol. Chem. 2002; 277: 33913-33921.
18. Braunstein A, Papo N, Shai Y. In vitro activity and potency of an intravenously injected antimicrobial peptide and its DL amino acid analog in mice infected with bacteria. Antimicrob. Agents Chemother. 2004; 48: 3127-3129.
19. Zhu WL, Nan YH, Hahm KS, Shin SY. Cell selectivity of an antimicrobial peptide melittin diastereomer with D-amino acid in the leucine zipper sequence. J. Biochem. Mol. Biol. 2007; 40: 1090-1094.
20. Wang P, Nan YH, Yang ST, Kang SW, Kim Y, Park IS, Hahm KS, Shin SY. Cell selectivity and anti-inflammatory activity of a Leu/Lys-rich α-helical model antimicrobial peptide and its diastereomeric peptides. Peptides 2010; 31: 1251-1261.
21. Cannon RD, Holmes AR, Mason AB, Monk BC. Oral candida: clearance, colonization or candidiasis? J. Dent. Res. 1995; 74: 1152-1161.
22. Odds FC. Candida infections: an overview. Crit. Rev. Microbiol. 1987; 15: 1-5.
23. Prasad R, Kapoor K. Multidrug resistance in yeast Candida. Int. Rev. Cytol. 2005; 242: 215-248.
24. Mochon AB, Liu H. The antimicrobial peptide histatin-5 causes a spatially restricted disruption on the Candida albicans surface, allowing rapid entry of the peptide into the cytoplasm. PLoS Pathog. 2008; 4: 1-12.
25. Viejo-Díaz M, Andrés MT, Fierro JF. Different anti-Candida activities of two human lactoferrin-derived peptides, Lfpep and Kaliocin-1. Antimicrob. Agents Chemother. 2005; 49: 2583-2588.
26. Benincasa M, Scocchi M, Pacor S, Tossi A, Nobili D, Basaglia G, Busetti M, Gennaro R. J. Antimicrob. Chemother. 2006; 58: 950-959.
27. Shai Y. Bach D, Yanovsky A. Channel formation properties of synthetic pardaxin and analogues. J. Biol. Chem. 1990; 265: 20202-20209.
28. Avrahami D, Shai Y. Conjugation of a magainin analogue with lipophilic acids controls hydrophobicity, solution assembly, and cell selectivity. Biochemistry 2002; 41: 2254-2263.
29. Makovitzki A, Avrahami D, Shai Y. Ultrashort antibacterial and antifungal lipopeptides. Proc. Nat. Acad. Sci. U.S.A. 2006; 103: 15997-6002.
30. Verkleij AJ, Zwaal RF, Roelofsen B, Comfurius P, Kastelijn D, Deenen LV. The asymmetric distribution of phospholipids in the human red cell membrane. A combined study using phospholipases and freeze-etch electron microscopy. Biochim. Biophys. Acta. 1973; 323: 178-193.
31. Mao D, Wallace BA. Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles. Biochemistry 1984; 23: 2667-2673.
32. De Kroon AI, Soekarjo MW, De Gier J, De Kruijff B. The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers. Biochemistry 1990; 29: 8229-8240.
33. Zhao H, Kinnunen PK. Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. J. Biol. Chem. 2002; 277: 25170-25177.
34. Barlett CR. Phosphorus assay in column chromatography. J. Biol. Chem. 1959; 234: 466-468.