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References

  • 1
    Lazarus, L.H. & Attila, M. (1993) The toad, ugly and venomous, wears yet a precious jewel in his skin. Prog. Neurobiol. 41, 473 507.
  • 2
    Erspamer, V. (1994) Bioactive secretions of the amphibian integument. In: Amphibian Biology. The Integument, 1, (H. Heatwole, ed.), pp. 178 350. Surrey, Beatty and Sons, Chipping Norton, New South Wales, Australia.
  • 3
    Bevins, C.L. & Zasloff, M. (1990) Peptides from frog skin. Annu. Rev. Biochem. 59, 395 414.
  • 4
    Barra, D. & Simmaco, M. (1995) Amphibian skin: a promising resource for antimicrobial peptides. Trends Biotech. 13, 205 209.
  • 5
    Steinborner, S.T., Currie, G.J., Bowie, J.H., Wallace, J.C., Tyler, M.J. (1998) New antibiotic caerin 1 peptides from the skin secretions of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria. J. Peptide Res. 51, 121 126.
  • 6
    Bowie, J.H., Wegener, K.L., Chia, B.C.S., Wabnitz, P.A., Carver, J.A., Tyler, M.J., Wallace, J.C. (1999) Host defence antibacterial peptides from skin secretions of Australian amphibians. The relationship between structure and activity. Protein Peptide Lett. 6, 259 269.
  • 7
    Chia, B.C.S., Carver, J.A., Mulhern, T.D., Bowie, J.H. (2000) Maculatin 1.1. An antimicrobial peptide from the Australian tree frog Litoria genimaculata; solution structure and biological activity. Eur. J. Biochem. 267, 1894 1908.
  • 8
    Wegener, K.L., Wabnitz, P.A., Carver, J.A., Bowie, J.H., Chia, B.C.S., Wallace, J.C., Tyler, M.J. (1999) Host defence peptides from the skin glands of the Australian Blue Mountains tree-frog Litoria citropa. Eur. J. Biochem. 265, 627 635.DOI: 10.1046/j.1432-1327.1999.00750.x
  • 9
    Bradford, A.M., Bowie, J.H., Tyler, M.J., Wallace, J.C. (1996) New antibiotic peptides from the dorsal glands of the Australian toadlet Uperoleia mjobergii. Aust. J. Chem. 49, 1325 1331.
  • 10
    Wong, H., Bowie, J.H., Carver, J.A. (1997) The solution structure and activity of caerin 1.1, an antimicrobial peptide from the Australian tree frog, Litoria splendida. Eur. J.Biochem. 247, 545 557.
  • 11
    Chia, B.C.S., Mulhern, T.D., Carver, J.A., Bowie, J.H. (1999) The solution structure of uperin 3.6, an antibiotic peptide from the granular dorsal glands of the Australian toadlet, Uperoleia mjobergii. J. Peptide. Res. 54, 137 145.
  • 12
    Arseniev, A.S., Barsukov, V.F., Bystro, V., Lomize, A.L., Ovchinnikov, Y.A. (1985) 1H-NMR study of gramicidin A transmembrane ion channel: head-to-head right-handed, single-stranded helices. FEBS Lett. 186, 168 174.
  • 13
    Marion, D., Zasloff, M., Bax, A. (1988) A two-dimensional NMR study of the antimicrobial peptide magainin 2. FEBS Lett. 227, 21 26.
  • 14
    Shai, Y. (1995) Molecular recognition between membrane-spanning peptides. Trends Biochem. Sci. 20, 460 464.
  • 15
    Epand, R.M., Shai, Y.C., Segrest, J.P., Anantharamaiah, G.M. (1995) Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides. Biopolymers 37, 319 338.
  • 16
    Bechinger, B. (1997) Structure and function of channel forming peptides, magainins, cecropins, melittin and alamethicin. J. Membr. Biol. 156, 197 211.DOI: 10.1007/s002329900201
  • 17
    Matsuzaki. K. (1998) Magainins as paradigm for the mode of action of pore forming polypeptides. Biochim. Biophys. Acta 1376, 391 400.
  • 18
    Bechinger, B., Zasloff, M., Opella, S.J. (1993) Structure and orientation of the antibiotic peptide magainin in membranes by solid-state NMR. Protein Sci. 2, 2077 2084.
  • 19
    Barker, J., Grigg, G.C., Tyler, M.J. (1995) A Field Guide to Australian Frogs. Surrey, Beatty and Sons, Chipping Norton, New South Wales, Australia.
  • 20
    Lesson, R.P. (1829) Description de quelques reptiles nouveaux ou peu connus. In: Duperrey, L.I (edn 1826–1838) Voyage autour du monde, executé par ordre du Roi, sur la corvette de sa Majesté, La Coquille, pendant les annees 1822, 1823, 1824 et 1825. Zoologie 2, 34 65, Arthus Bertrand, Paris.
  • 21
    Kerferstein, W. (1867) Ueber einige neue oder seltene Batrachier aus Australien und dem tropischen Amerika. Nachr. Ges. Wiss. Göttingen. 341 361.
  • 22
    Tyler, M.J., Stone, D.J.M., Bowie, J.H. (1992) A novel method for the release and collection of dermal glandular secretions from the skin of frogs. J. Pharmacol. Toxicol. Methods 28, 199 200.
  • 23
    Hunkapiller, M.W., Hewick, R.M., Drewer, W.J., Hood, L.E. (1983) High-sensitivity sequencing with a gas-phase sequencer. Methods Enzymol. 91, 399 406.
  • 24
    Maeji, N.J., Bray, R.M., Valerio, R.M., Wang, W. (1995) Larger scale multipin peptide synthesis. Peptide Res. 8, 33 38.
  • 25
    Jorgensen, J.H., Cleeland, W.A., Craig, G., Doern, M., Ferraro, J., Finegold, C.M., Hansen, S.L., Jenkins, S.G., Novick, W.J., Pfaller, M.A., Preston, D.A., Reller, L.B., Swenson, J.M. (1993) Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically, 3rd approved standard. Natl. Committee Clin. Lab. Stand. 13, 1 12. Document M7–A3.
  • 26
    Developmental Therapeutics Program (http://dtp.nci.nih.gov). National Cancer Institute, Washington, DC, USA.
  • 27
    Rance, M., Sørrenson, O.W., Bodenhausen, G., Wagner, G., Ernst, R.R., Wüthrich, K. (1983) Improved spectral resolution in COSY 1H-NMR spectra of proteins via double quantum filtering. Biochem. Biophys. Res. Commun. 117, 479 485.
  • 28
    Davis, D.G. & Bax, A. (1985) Assignment of complex 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J. Am. Chem. Soc. 107, 2820 2821.
  • 29
    Jeener, J., Meier, B.H., Bachman, P., Ernst, R.R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546 4553.
  • 30
    Marion, D. & Wüthrich, K. (1983) Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 113, 967 974.
  • 31
    John, B.K., Plant, D., Webb, P., Hurd, R.E. (1992) Effective combination of gradients and crafted RF pulses for water suppression in biological samples. J. Magn. Reson. 98, 200 206.
  • 32
    Griesinger, C., Otting, G., Wüthrich, K., Ernst, R.R. (1988) Clean TOCSY for 1H spin system identification in macromolecules. J. Am. Chem. Soc. 110, 7870 7872.
  • 33
    Kay, L.E., Keifer, P., Saaringen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663 10665.
  • 34
    Summers, M.F., Marzilli, L.G., Bax, A. (1986) Complete 1H and 13C assignments of coenzyme B12 through the use of new two-dimensional NMR experiments. J. Am. Chem. Soc. 108, 4285 4294.
  • 35
    Bartels, C., Xia, T.H., Billeter, M., Güntert, P., Wüthrich, K. (1995) The program XEASY for computer supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 6, 1 10.
  • 36
    Xu, R.X., Word, J.M., Davis, D.G., Rink, M.J., Willard, D.H., Gampe, R.T. (1995) Solution structure of the human pp. 60c-src SH2 domain complexed with a phosphorylated tyrosine pentapeptide. Biochemistry 34, 2107 2121.
  • 37
    Brunger, A.T. (1992) A system for X-ray crystallography and NMR. In X-PLOR (Version 3.851). Yale University, New Haven, CT, USA.
  • 38
    Brunger, A.T. & Nilges, M. (1993) Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMR-spectroscopy. Q. Rev. Biophys. 26, 49 125.
  • 39
    Nilges, M., Kuszewski, J., Brunger, A.T. (1992) Sampling properties of simulated annealing. In Proceedings of the NATO Advanced Research Workshop on Computational Aspects of the Study of Biological Macromolecules by NMR. Il Ciocco, Italy.
  • 40
    Folmer, R.H.A., Hilbers, C.W., Konings, R.N.H., Nilges, M. (1997) Floating stereospecific assignment revisited – application to an 18 kDa protein and comparison with J-coupling data. J. Biomol. NMR 9, 245 258.
  • 41
    Engh, R.A. & Huber, R. (1991) Accurate bond and angle parameters for x-ray protein structure refinement. Acta Crystallogr. A 47, 392 400.
  • 42
    Koradi, R., Billeter, M., Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51 55.
  • 43
    Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids. Wiley. New York, USA.
  • 44
    Wishart, D.S., Bigam, C.G., Holm, A., Hodges, R.S., Sykes, B.D. (1995) 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbour effects. J. Biomol. NMR 5, 67 81.
  • 45
    Pastore, A. & Saudek, V. (1990) The relationship between chemical shift and secondary structure. J. Magn. Reson. 90, 165 176.
  • 46
    Wishart, D.S., Richards, F.M., Sykes, B.D. (1991) Relationship between NMR chemical shift and protein secondary structure. J. Mol. Biol. 222, 311 333.
  • 47
    Wishart, D.S., Richards, F.M., Sykes, B.D. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647 1651.
  • 48
    Wishart, D.S. & Sykes, B.D. (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR 4, 171 180.
  • 49
    Pallaghy, P.K., Duggan, B.M., Pennington, M.W., Norton, R.S. (1993) 3-Dimensional structure in solution of the calcium channel blocker ω-conotoxin. J. Mol. Biol. 234, 405 420.
  • 50
    Morris, A.L., MacArthur, M.W., Hutchinson, E.G., Thornton, J.M. (1992) Stereochemical quality of protein structure coordinates. Proteins 12, 345 364.
  • 51
    Alvarezbravo, J., Kurata, S., Natori, S. (1995) Mode of action of an antibacterial peptide KLKLLLLLKLK-NH2. Biochem. J. 117, 1312 1316.
  • 52
    Saido-Sakanata, H. & Ishibashi, J. (1999) Synthesis and characterisation of bacterial oligopeptides designed on the basis of an insect anti-bacterial peptide. Biochem. J. 338, 19 33.
  • 53
    Lawyer, C., Pai, S., Watabe, M., Borgia, P., Eagleton, L., Watabe, K. (1996) Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides. FEBS Lett. 390, 95 98.
  • 54
    Guttman, S.I. (1973) Biochemical techniques and problems in anuran evolution. In Evolutionary Biology of the Anurans: Contempory Research on Major Problems (Vial, J.L., ed.), pp. 183 203. University of Missouri Press, Columbia, OH, USA.
  • 55
    Duellman, W.E. & Trueb, L. (1986) Biology of Amphibians. McGraw-Hill. New York, USA.
  • 56
    Ganz, T. (1994) Biosynthesis of defensins and other antimicrobial peptides. Antimicrobial Peptides. Ciba Symposium 186 ( Boman, H.G., Marsh, J. & Goode J.A., eds.), pp. 62 76. Wiley, Chichester, UK.
  • 57
    Resnick, N., Maloy, W., Crut, H., Zasloff, M. (1991) A novel endopeptidase from Xenopus that recognises α-helical structure. Cell 66, 541 554.
  • 58
    Tieleman, D.P., Sansom, M.S.P., Berendsen, H.J.C. (1999) Alamethicin helices in a bilayer and in solution: a molecular dynamics simulation study. Biophys. J. 76, 40 49.
  • 59
    Gazit, E., Miller, I.R., Biggin, P.C., Sansom, M.S.P., Shai, Y. (1996) Structure and orientation of the antimicrobial peptide cecropin p1 within phospholipid membranes. J. Mol. Biol. 258, 860 870.
  • 60
    Arseniev, A.S., Barsukov, I.L., Bystrov, V.F., Lomize, A.L., Ovchinnikov, YU. A. (1985) 1H NMR study of granimicidin A transmembrane ion channels. FEBS Lett. 186, 168 173.
  • 61
    Strahilevitz, J., Mor, A., Nicolas, P., Shai, Y. (1994) Spectrum of antimicrobial activity and assembly of dermaseptin b and its precursor form in phospholipid membranes. Biochemistry 33, 10951 10960.
  • 62
    Ludke, S.J., He, K., Huang, H.W. (1995) Membrane thinning caused by magainin 2. Biochemistry 34, 16764 16769.
  • 63
    Smith, R., Separovic, F., Milne, T.J., Whittacher, A., Bennett, F.M., Cornell, B.A., Makriyannis, A. (1994) Structure and orientation of the pore-forming peptide, melitten, in lipid bilayers. J. Mol. Biol. 241, 456 466.
  • 64
    Baker, M.A., Maloy, W.L., Zasloff, M., Jacob, L.S. (1993) Anticancer efficacy of Magainin2 and analogue peptides. Cancer. Res. 53, 3052 3057.
  • 65
    Zubay, G. (1986) Biochemistry. Addison-Wesley Publishers Co, Massachussetts, USA.
  • 66
    Conner, J., Bucana, C., Fidler, I.J., Schroit, A.J. (1989) Differentiation dependent expression of phosphatidyl serine in mammalian plasma membranes: quantitative assessment of outer-leaflet lipid by prothrombin complex formation. Proc. Natl Acad. Sci. USA 86, 3184 3188.
  • 67
    Utsugi, T., Schroit, A.J., Conner, J., Bucana, C., Fidler, I.J. (1991) Elevated expression of phosphatidyl serine in the outer membrane leaflet of human tumor cells and recognition of activated human blood monocycles. Cancer Res. 51, 3062 3066.
  • 68
    Tytler, E.M., Anantharamaiah, G.M., Walker, D.E., Mishra, V.K., Palgunachari, M.N., Segrest, J.P. (1995) Molecular basis for prokaryotic specificity of magainin-induced lysis. Biochemistry. 34, 4393 4401.
  • 69
    Wabnitz, P.A., Bowie, J.H., Tyler, M.J., Wallace, J.C., Smith, B.P. (1999) Aquatic sex pheromone from a male frog. Nature (Lond.) 401, 444 445.
  • 70
    Wabnitz, P.A., Bowie, J.H., Tyler, M.J., Wallace, J.C., Smith, B.P. (2000) Differences in skin peptides of the male and female Australian magnificent tree frog Litoria splendida– a three year monitoring survey: the discovery of the aquatic male sex pheromone splendipherin, together with phe8 caerulein and the antibiotic caerin 1.10. Eur. J. Biochem. 267, 269 275.
  • 71
    Sönnichsen, F.D., Van Eyk, J.E., Hodges, R.S., Sykes, B.D. (1992) Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry 31, 8790 8798.
  • 72
    Dyson, H.J., Merutka, G., Waltho, J.P., Lerner, R.A., Wright, P.E. (1992) Folding of peptide fragments comprising the complete sequence of proteins; modes for initiation of protein folding. 1. Myohemerhthrin. J. Mol. Biol. 226, 795 817.