Development of potent anti-infective agents from Silurana tropicalis: Conformational analysis of the amphipathic, alpha-helical antimicrobial peptide XT-7 and its non-haemolytic analogue [G4K]XT-7

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1804, Issue 4, 2010, Pages 1020-1028

  Subasinghage, Anusha P ^a   Conlon, J Michael ^b   Hewage, Chandralal M ^a  

^a University College Dublin   (Ireland)

^b UNITED ARAB EMIRATES UNIVERSITY   (United Arab Emirates)

Author keywords

Amphipathic helix; Antimicrobial; NMR; Silurana tropicalis; XT 7

Indexed keywords

ANTIINFECTIVE AGENT; ANTIMICROBIAL PEPTIDE [G4K]XT 7; ANTIMICROBIAL PEPTIDE XT 7; POLYPEPTIDE ANTIBIOTIC AGENT; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANTIMICROBIAL ACTIVITY; AQUEOUS SOLUTION; ARTICLE; CANDIDA ALBICANS; CONFORMATIONAL TRANSITION; DRUG POTENCY; DRUG STRUCTURE; ESCHERICHIA COLI; FROG; HEMOLYSIS; HUMAN; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SILURANA TROPICALIS; STAPHYLOCOCCUS AUREUS; TOAD;

AMINO ACID SEQUENCE; AMPHIBIAN PROTEINS; ANIMALS; ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; HEMOLYSIS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; RANIDAE;

ANURA; PIPIDAE; XENOPUS TROPICALIS;

EID: 77149153393     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.01.015     Document Type: Article

References (38)

1. Nicolas P., Vanhoye D., and Amiche M. Molecular strategies in biological evolution of antimicrobial peptides. Peptides 24 (2003) 1669-1680
2. Conlon J.M., Kolodziejek J., and Nowotny N. Antimicrobial peptides from the skins of North American frogs. Biochim. Biophys. Acta 1788 (2009) 1556-1563
3. Yeaman M.R., and Yount N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55 (2003) 27-55
4. Risso A., Braidot E., Sordano M.C., Vianello A., Macri F., Skerlavaj B., Zanetti M., Gennaro R., and Bernardi P. BMAP-28, an antibiotic peptide of innate immunity, induces cell death through opening of the mitochondrial permeability transition pore. Mol. Cell. Biol. 22 (2002) 1926-1935
5. Rinaldi A.C. Antimicrobial peptides from amphibian skin: an expanding scenario. Curr. Opin. Chem. Biol. 6 (2002) 799-804
6. Papo N., and Shai Y. Host defense peptides as new weapons in cancer treatment. Cell. Mol. Life Sci. 62 (2005) 784-790
7. Ali M.F., Soto A., Knoop F.C., and Conlon J.M. Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae). Biochim. Biophys. Acta 1550 (2001) 81-89
8. Conlon J.M., Galadari S., Raza H., and Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7. Chem. Biol. Drug Des. 72 (2008) 58-64
9. Giangaspero A., Sandri L., and Tossi A. Amphipathic alpha helical antimicrobial peptides. Eur. J. Biochem. 268 (2001) 5589-5600
10. Bax A., and Davis D.G. MLEV-17 based two-dimentional homonuclear magnetisation transfer spectroscopy. J. Magon. Reson. 65 (1985) 355-360
11. Kumar A., Ernst R.R., and Wuthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95 (1980) 1-6
12. T.D. Goddard, D.G. Kneller, Sparky 3 software, University of California, San Francisco, USA, 2006.
13. Guntert P., Braun W., and Wuthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217 (1991) 517-530
14. Guntert P., Mumenthaler C., and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273 (1997) 283-298
15. Tripos Inc., 1699 South Janley Road, St. Louis, MO 63144-2319, USA.
16. Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 51-55 (1996) 29-32
17. Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
18. Wishart D.S., and Nip A.M. Protein chemical shift analysis: a practical guide. Biochem. Cell Biol. 76 (1998) 153-163
19. Schibli D.J., Nguyen L.T., Kernaghan S.D., Rekdal O., and Vogel H.J. Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures. Biophys. J. 91 (2006) 4413-4426
20. Friedrich C.L., Moyles D., Beveridge T.J., and Hancock R.E. Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria. Antimicrob. Agents Chemother. 44 (2000) 2086-2092
21. Eley A., Ibrahim M., Kurdi S.E., and Conlon J.M. Activities of the frog skin peptide, ascaphin-8 and its lysine-substituted analogs against clinical isolates of extended-spectrum beta-lactamase (ESBL) producing bacteria. Peptides 29 (2008) 25-30
22. Rinaldi A.C. Antimicrobial peptides from amphibian skin: an expanding scenario. Curr. Opin. Chem. Biol. 6 (2002) 799-804
23. Sonnichsen F.D., Van Eyk J.E., Hodges R.S., and Sykes B.D. Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry 31 (1992) 8790-8798
24. Alana I., Malthouse J.P., O'Harte F.P., and Hewage C.M. The bioactive conformation of glucose-dependent insulinotropic polypeptide by NMR and CD spectroscopy. Proteins 68 (2007) 92-99
25. Subasinghage A.P., Conlon J.M., and Hewage C.M. Conformational analysis of the broad-spectrum antibacterial peptide, ranatuerin-2CSa: identification of a full length helix-turn-helix motif. Biochim. Biophys. Acta 1784 (2008) 924-929
26. Hewage C.M., Jiang L., Parkinson J.A., Ramage R., and Sadler I.H. A linear endothelin-1 analogue: solution structure of ET-1[Aib1, 3, 11, 15, Nle7] by nuclear magnetic resonance spectroscopy and molecular modelling. Neurochem. Int. 35 (1999) 35-45
27. Conlon J.M., Galadari S., Raza H., and Condamine E. Design of potent, non-toxic antimicrobial agents based upon the naturally occurring frog skin peptides, ascaphin-8 and peptide XT-7. Chem. Biol. Drug Des. 72 (2008) 58-64
28. Powers J.P., and Hancock R.E. The relationship between peptide structure and antibacterial activity. Peptides 24 (2003) 1681-1691
29. Yeaman M.R., and Yount N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55 (2003) 27-55
30. Conlon J.M., Al-Ghaferi N., Abraham B., and Leprince J. Strategies for transformation of naturally-occurring amphibian antimicrobial peptides into therapeutically valuable anti-infective agents. Methods 42 (2007) 349-357
31. Dathe M., Schumann M., Wieprecht T., Winkler A., Beyermann M., Krause E., Matsuzaki K., Murase O., and Bienert M. Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 35 (1996) 12612-12622
32. Dathe M., and Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1462 (1999) 71-87
33. Wieprecht T., Dathe M., Beyermann M., Krause E., Maloy W.L., MacDonald D.L., and Bienert M. Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry 36 (1997) 6124-6132
34. Tachi T., Epand R.F., Epand R.M., and Matsuzaki K. Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity. Biochemistry 41 (2002) 10723-10731
35. Chen Y., Mant C.T., Farmer S.W., Hancock R.E., Vasil M.L., and Hodges R.S. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J. Biol. Chem. 280 (2005) 12316-12329
36. Dathe M., Wieprecht T., Nikolenko H., Handel L., Maloy W.L., MacDonald D.L., Beyermann M., and Bienert M. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Lett. 403 (1997) 208-212
37. Wieprecht T., Dathe M., Krause E., Beyermann M., Maloy W.L., MacDonald D.L., and Bienert M. Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment. FEBS Lett. 417 (1997) 135-140
38. Maloy W.L., and Kari U.P. Structure-activity studies on magainins and other host defense peptides. Biopolymers 37 (1995) 105-122