An unusual peptide from Conus villepinii: Synthesis, solution structure, and cardioactivity

Peptides

Volumn 31, Issue 7, 2010, Pages 1292-1300

  Miloslavina, Alesia ^a   Ebert, Christina ^b   Tietze, Daniel ^b   Ohlenschläger, Oliver ^c   Englert, Christoph ^b   Görlach, Matthias ^c   Imhof, Diana ^a  

^a Center for Molecular Biomedicine   (Germany)

^b FRITZ LIPMANN INSTITUTE   (Germany)

^c DARMSTADT UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

Cardioactivity; Conopeptide; Ionic liquids; NMR solution structure; Oxidation; Zebrafish embryos

Indexed keywords

CRUSTACEAN CARDIOACTIVE PEPTIDE; IONIC LIQUID; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; CONUS SNAIL; DRUG STRUCTURE; DRUG SYNTHESIS; EMBRYO; HEART RATE; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SOLID PHASE SYNTHESIS; ZEBRA FISH;

AMINO ACID SEQUENCE; ANIMALS; CONOTOXINS; CONUS SNAIL; EMBRYO, NONMAMMALIAN; HEART RATE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOPEPTIDES; PEPTIDES, CYCLIC; PROTEIN CONFORMATION; ZEBRAFISH;

ANIMALIA; ARTHROPODA; CONUS VILLEPINII; DANIO RERIO; GASTROPODA;

EID: 77952553212     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2010.04.002     Document Type: Article

References (53)

1. Barbar E., Barany G., and Woodward C. Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink 1. Fold Des 1 (1996) 65-76
2. Bartels C., Xia T.-H., Billeter M., Günterl P., and Wüthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J Biomol NMR 5 (1995) 1-10
3. Burnison B.K., Meinelt T., Playle R., Pietrock M., Wienke A., and Steinberg C.E. Cadmium accumulation in zebrafish (Danio rerio) eggs is modulated by dissolved organic matter (DOM). Aquat Toxicol (Amsterdam, Netherlands) 79 (2006) 185-191
4. Constantinescu D., Weingartner H., and Herrmann C. Protein denaturation by ionic liquids and the Hofmeister series: a case study of aqueous solutions of ribonuclease A. Angew Chem Int Ed 46 (2007) 8887-8889
5. Craig A.G., Norberg T., Griffin D., Hoeger C., Akhtar M., Schmidt K., et al. Contulakin-G, an O-glycosylated invertebrate neurotensin. J Biol Chem 274 (1999) 13752-13759
6. DeLa Cruz R., Whitby F.G., Buczek O., and Bulaj G. Detergent-assisted oxidative folding of delta-conotoxins. J Pept Res 61 (2002) 202-212
7. Dircksen H. Conserved crustacean cardioactive peptide (CCAP) neuronal networks and functions in arthropod evolution. In: Coast G.M., and Webster S.G. (Eds). Recent advances in arthropod endocrinology (1998), Cambridge University Press, London 302-334
8. Dulcis D., Levine R.B., and Ewer J. Role of the neuropeptide CCAP in Drosophila cardiac function. J Neurobiol 64 (2005) 259-274
9. Ellman G.L. A colorimetric method for determining low concentrations of mercaptans. Arch Biochem Biophys 74 (1958) 443-450
10. Ellman G.L. Tissue sulfhydryl groups. Arch Biochem Biophys 82 (1959) 70-77
11. Gellert G., and Heinrichsdorff J. Effect of age on the susceptibility of zebrafish eggs to industrial wastewater. Water Res 35 (2001) 3754-3757
12. Güntert P., Billeter M., Ohlenschläger O., Brown L.R., and Wüthrich K. Conformation analysis of protein and nucleic acid fragments with the new grid search algorithm FOUND. J Biomol NMR 12 (1998) 543-548
13. Herrmann T., Guntert P., and Wuthrich K. Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR 24 (2002) 171-189
14. Hofmeister F. Zur Lehre von der Wirkung der Salze. Zweite Mittheilung. Arch Exp Pathol Pharmakol 24 (1888) 247-260
15. Jackson G.E., Mabula A.N., Stone S.R., Gade G., Kover K.E., Szilagyi L., et al. Solution conformations of an insect neuropeptide: crustacean cardioactive peptide (CCAP). Peptides 30 (2009) 557-564
16. Kimmel C.B., Ballard W.W., Kimmel S.R., Ullmann B., and Schilling T.F. Stages of embryonic development of the zebrafish. Dev Dyn 203 (1995) 253-310
17. Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14 (1996) 51-5, 29-32
18. Korbas M., Blechinger S.R., Krone P.H., Pickering I.J., and George G.N. Localizing organomercury uptake and accumulation in zebrafish larvae at the tissue and cellular level. Proc Natl Acad Sci USA 105 (2008) 12108-12112
19. Kotelchuck D., Scheraga H.A., and Walter R. Conformational energy studies of oxytocin and its cyclic moiety. Proc Natl Acad Sci USA 69 (1972) 3629-3633
20. Lewis P.N., Momany F.A., and Scheraga H.A. Chain reversals in proteins. Biochim Biophys Acta 303 (1973) 211-229
21. Loi P.K., Emmal S.A., Park Y., and Tublitz N.J. Identification, sequence and expression of a crustacean cardioactive peptide (CCAP) gene in the moth Manduca sexta. J Exp Biol 204 (2001) 2803-2816
22. Luginbuhl P., Guntert P., Billeter M., and Wuthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules. J Biomol NMR 8 (1996) 136-146
23. Lungwitz R., and Spange S. A hydrogen bond accepting (HBA) scale of anions, including room temperature ionic liquids. New J Chem 32 (2008) 392-394
24. Lyons M.S., Bell B., Stainier D., and Peters K.G. Isolation of the zebrafish homologues for the tie-1 and tie-2 endothelium-specific receptor tyrosine kinases. Dev Dyn 212 (1998) 133-140
25. Mari F., and Fields G.B. Conopeptides: unique pharmacological agents that challenge current peptide methodologies. Chimica Oggi 21 (2003) 43-48
26. McGaw I.J., Airriess C.N., and McMahon B.R. Peptidergic modulation of cardiovascular dynamics in the Dungeness crab, Cancer magister. J Comp Physiol B 164 (1994) 103-111
27. McIntosh J.M., Hasson A., Spira M.E., Gray W.R., Li W.Q., Marsh M., et al. A new family of conotoxins that blocks voltage-gated sodium-channels. J Biol Chem 270 (1995) 16796-16802
28. Miloslavina A.A., Leipold E., Kijas M., Stark A., Heinemann S.H., and Imhof D. A room temperature ionic liquid as convenient solvent for the oxidative folding of conopeptides 1. J Pept Sci 15 (2009) 72-77
29. Moller C., Melaun C., Marks V., Dovel S., Diaz M., and Mari F. J Pept Sci Suppl 14 (2008) 19
30. Moller C., Rahmankhah S., Lauer-Fields J., Bubis J., Fields G.B., and Mari F. A novel conotoxin framework with a helix-loop-helix (Cs alpha/alpha) fold. Biochemistry 44 (2005) 15986-15996
31. Muneoka K., Mikuni M., Ogawa T., Kitera K., and Takahashi K. Periodic maternal deprivation-induced potentiation of the negative feedback sensitivity to glucocorticoids to inhibit stress-induced adrenocortical-response persists throughout the animals life-span 6. Neurosci Lett 168 (1994) 89-92
32. Nagata K., and Tanokura M. Cardioacceleratory peptide (CCAP) of the fruit fly Drosophila melanogaster: solution structure analysis and docking simulation to the receptor CG6111. Pept Sci 41 (2005) 441-444
33. Nelson K.J., Day A.E., Zeng B.B., King S.B., and Poole L.B. Isotope-coded, iodoacetamide-based reagent to determine individual cysteine pK(a) values by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal Biochem 375 (2008) 187-195
34. Norton R.S., and Olivera B.M. Conotoxins down under. Toxicon 48 (2006) 780-798
35. Pawlukojc A., Leciejewicz J., Ramirez-Cuesta A.J., and Nowicka-Scheibe J. l-Cysteine: neutron spectroscopy, Raman, IR and ab initio study. Spectrochim Acta 61 (2005) 2474-2481
36. Phillips D.M., Drummy L.F., Conrady D.G., Fox D.M., Naik R.R., Stone M.O., et al. Dissolution and regeneration of Bombyx mori silk fibroin using ionic liquids. JACS 126 (2004) 14350-14351
37. Roex E.W., de Vries E., and van Gestel C.A. Sensitivity of the zebrafish (Danio rerio) early life stage test for compounds with different modes of action. Environ Pollut 120 (2002) 355-362
38. Schlucker S., Liang C., Strehle K.R., DiGiovanna J.J., Kraemer K.H., and Levin I.W. Conformational differences in protein disulfide linkages between normal hair and hair from subjects with trichothiodystrophy: a quantitative analysis by Raman microspectroscopy. Biopolymers 82 (2006) 615-622
39. Schmidt J.M., Ohlenschlager O., Ruterjans H., Grzonka Z., Kojro E., Pavo I., et al. Conformation of [8-arginine]vasopressin and V1 antagonists in dimethyl sulfoxide solution derived from two-dimensional NMR spectroscopy and molecular dynamics simulation. Eur J Biochem 201 (1991) 355-371
40. Slama K., Sakai T., and Takeda M. Effect of corazonin and crustacean cardioactive peptide on heartbeat in the adult American cockroach (Periplaneta americana). Arch Insect Biochem Physiol 62 (2006) 91-103
41. Stangier J., Hilbich C., Beyreuther K., and Keller R. Unusual cardioactive peptide (CCAP) from pericardial organs of the shore crab Carcinus maenas. Proc Natl Acad Sci USA 84 (1987) 575-579
42. Swatloski R.P., Spear S.K., Holbrey J.D., and Rogers R.D. Dissolution of cellose with ionic liquids. JACS 124 (2002) 4974-4975
43. Terlau H., and Olivera B.M. Conus venoms: a rich source of novel ion channel-targeted peptides. Physiol Rev 84 (2004) 41-68
44. Tu T., Tu A.T., and Lin T.S. Some pharmacological properties of the venom, venom fractions and pure toxin of the yellow-bellied sea snake Pelamis platurus. J Pharm Pharmacol 28 (1976) 139-145
45. Vehovszky A., Agricola H.J., Elliott C.J.H., Ohtani M., Karpati L., and Hernadi L. Crustacean cardioactive peptide (CCAP)-related molluscan peptides (M-CCAPs) are potential extrinsic modulators of the buccal feeding network in the pond snail Lymnaea stagnalis 2. Neurosci Lett 373 (2005) 200-205
46. Wang C.Z., and Chi C.W. Conus peptides-a rich pharmaceutical treasure. Acta Biochim Biophys Sin 36 (2004) 713-723
47. Wasielewski O., and Skonieczna M. Pleiotropic effects of the neuropeptides CCAP and myosuppressin in the beetle, Tenebrio molitor L. J Comp Physiol 178 (2008) 877-885
48. Westerfield M. The zebrafish book; a guide for the laboratory use of zebrafish (Brachydanio rerio). 2nd ed. (1993), University of Oregon Press, Eugene
49. 1H nuclear magnetic resonance and distance geometry. J Mol Biol 182 (1985) 295-315
50. Zhao H. Effect of ions and other compatible solutes on enzyme activity, and its implication for biocatalysis using ionic liquids. J Mol Catal B: Enzym 37 (2005) 16-25
51. Zhao H., Campbell S.M., Jackson L., Song Z., and Olubajo O. Hofmeister series of ionic liquids: kosmotropic effect of ionic liquids on the enzymatic hydrolysis of enantiomeric phenylalanine methyl ester. Tetrahedr: Asymm 17 (2006) 377-383
52. Zhao H., Olubajo O., Song Z., Sims A.L., Person T.E., Lawal R.A., et al. Effect of kosmotropicity of ionic liquids on the enzyme stability in aqueous solutions. Bioorg Chem 34 (2006) 15-25
53. Zorn S., Leipold E., Hansel A., Bulaj G., Olivera B.M., Terlau H., et al. The mu O-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3. FEBS Lett 580 (2006) 1360-1364