Phalloidin synthetic analogues: Structural requirements in the interaction with F-actin

Chemistry - A European Journal

Volumn 7, Issue 21, 2001, Pages 4665-4673

  Falcigno, Lucia ^a   Costantini, Susan ^a   D'Auria, Gabriella ^a   Bruno, Bianca Maria ^b   Zobeley, Suse ^c   Zanotti, Giancarlo ^b   Paolillo, Livio ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

^c MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

Atropisomerism; Conformation analysis; F actin; NMR spectroscopy; Phallotoxin analogues

Indexed keywords

DERIVATIVES; DOCKING; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLUTIONS;

CIRCULAR DICHROISMS;

INORGANIC COMPOUNDS;

ACTIN; BICYCLO COMPOUND; F ACTIN; PHALLOIDIN; PHALLOTOXIN; SYNTHETIC PEPTIDE;

ARTICLE; BINDING SITE; CHEMICAL INTERACTION; CHEMICAL STRUCTURE; CHEMISTRY; CHIRALITY; CIRCULAR DICHROISM; ISOMERISM; MOLECULAR DYNAMICS; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; SIMULATION; STRUCTURE ANALYSIS; SYNTHESIS; TOXICITY;

ACTINS; CIRCULAR DICHROISM; MODELS, MOLECULAR; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHALLOIDINE;

EID: 0035813669     PISSN: 09476539     EISSN: None     Source Type: Journal    
DOI: 10.1002/1521-3765(20011105)7:21<4665::AID-CHEM4665>3.0.CO;2-H     Document Type: Article

References (53)

1. T. Wieland, Peptides of Poisonous Amanita Mushrooms, Springer, New York, 1986.
2. M. Frimmer, Biol. Unserer Zeit 1979, 9, 147-152.
3. T. Wieland, Naturwissenschaften 1977, 64, 303-309.
4. J. Vandekerckhove, A. Deboden, M. Nassal, T. Wieland, EMBO J. 1985, 4, 2815-2828.
5. P. Dancker, J. Low, W. Hasselbach, T. Wieland, Biochim. Biophys. Acta 1975, 400, 407-414.
6. J. Low, P. Dancker, T. Wieland, FEBS Lett. 1975, 54, 263-265.
7. J. De Vries, T. Wieland, Biochemistry 1978, 17, 1965-1968.
8. T. Wieland, B. Beijer, A. Seeliger, J. Dabrowski, G. Zanotti, A. E. Tonelli, A. Gieren, B. Dederer, V. Lamm, E. Haedicke, Liebigs Ann. Chem. 1981, 2318-2334.
9. G. Zanotti, L. Falcigno, M. Saviano, G. D'Auria, B. M. Bruno, T. Campanile, L. Paolillo, Chem. Eur. J. 2001, 7, 1479-1485.
10. N. Kobayashi, S. Endo, H. Kobayashi, H. Faulstich, T. Wieland, Eur. J. Biochem. 1995, 232, 726-736.
11. H. Kessler, T. Wein, Liebigs Ann. Chem. 1991, 179-184.
12. P. Boenzli, J. T. Gerig, J. Am. Chem. Soc. 1990, 112, 3719-3726.
13. E. Munekata, N. Kobayashi, S. Endo, H. Faulstich, T. Wieland, in Peptide Chemistry 1990 (Ed.: Y. Shimonishi), Osaka, 1991, pp. 333-338.
14. D. J. Patel, A. E. Tonelli, P. Pfaender, H. Faulstich, T. Wieland, J. Mol. Biol. 1973, 79, 185-196.
15. F. Fahrenholz, H. Faulstich, T. Wieland, Liebigs Ann. Chem. 1971, 743, 89-104.
16. E. Munekata, H. Faulstich, T. Wieland, J. Am. Chem. Soc. 1977, 99, 6151-6153.
17. E. Munekata, H. Faulstich, T. Wieland, Liebigs Ann. Chem. 1978, 776-784.
18. E. Munekata, H. Faulstich, T. Wieland, Liebigs Ann. Chem. 1979, 1020-1027.
19. T. Wieland, A. Deboden, H. Faulstich, Liebigs Ann. Chem. 1980, 416-424.
20. L. S. Barak, R. R. Yocum, Anal. Biochem. 1981, 110, 31-38.
21. H. Heber, H. Faulstich, T. Wieland, Int. J. Pept. Protein Res. 1974, 6, 381-384.
22. T. Wieland, T. Miura, A. Seeliger, Int. J. Pept. Protein Res. 1983, 21, 3-10.
23. W. E. Savige, Aust. J. Chem. 1975, 28, 2275-2287.
24. W. E. Savige, A. Fontana, J. Chem. Soc. Chem. Commun. 1976, 600-601.
25. W. E. Savige, A. Fontana, Int. J. Pept. Protein Res. 1980, 15, 102-112.
26. G. Zanotti, C. Birr, T. Wieland, Int. J. Pept. Protein Res. 1981, 18, 162-168.
27. G. Zanotti, C. Moebringer, T. Wieland, Int. J. Pept. Protein Res. 1987, 50, 450-459.
28. L. Braunschweiler, R. R. Ernst, J. Magn. Reson. 1983, 53, 521-528.
29. U. Piantini, O. W. Sørensen, R. R. Ernst, J. Am. Chem. Soc. 1982, 104, 6800-6801.
30. M. Ranee, O. W. Sørensen, G. Bodenhausen, G. Wagner, R. R. Ernst, K. Wüthrich, Biochem. Biophys. Res. Commun. 1983, 117, 479-485.
31. A. Bothner-By, R. L. Stephens, J.-M. Lee, C. D. Warren, R. Jeanloz, J. Am. Chem. Soc. 1984, 106, 811-813.
32. A. Bax, D. Davis, J. Magn. Reson. 1985, 63, 207-213.
33. A. Kumar, G. Wagner, R. R. Ernst, K. Wüthrich, J. Am. Chem. Soc. 1981, 103, 3654-3658.
34. D. Neuhaus, M. Williamson, The Nuclear Overhauser Effect in Structural Conformation Analysis, VCH, New York, 1989.
35. L. Mueller, J. Am. Chem. Soc. 1979, 101, 4481-4484.
36. A. Bax, R. H. Griffey, B. L. Hawkins, J. Magn. Reson. 1983, 55, 301-315.
37. K. Wüthrich, NMR of Proteins and Nucleic Acids, Wiley, New York, 1986.
38. V. F. Bystrov, Prog. Nucl. Magn. Reson. Spectrosc. 1976, 10, 41-82.
39. C. Isernia, L. Paolillo, E. Russo, A. L. Pastore, G. Zanotti, S. Macura, J. Biomol. NMR 1992, 2, 573-582.
40. G. D. Rose, L. M. Gierasch, J. A. Smith, in Advances in Protein Chemistry, Vol. 37 (Eds.: C. B. Anfisen, J. T. Edsael, F. M. Richards), Academic Press, Orlando, Florida, 1985, pp. 1-109.
41. M. Lorenz, D. Popp, K. C. Holmes, J. Mol. Biol. 1993, 234, 826-836.
42. W. Kabsch, H. G. Mannherz, D. Suck, E. Pai, K. C. Holmes, Nature 1990, 347, 37-44.
43. K. C. Holmes, D. Popp, W. Gebhard, W. Kabsch, Nature 1990, 347, 44-49.
44. M. O. Steinmetz, D. Stoffler, S. A. Müller, W. Jahn, B. Wolpensinger, K. N. Goldie, A. Engel, H. Faulstich, U. Aebi, J. Mol. Biol. 1998, 276, 1-6.
45. D. G. Drubin, H. D. Jones, K. F. Wertmann, Mol. Biol. Cell. 1993, 4, 1277-1294.
46. C. Griesinger, R. R. Ernst, J. Magn. Reson. 1987, 75, 261-271.
47. S. Lifson, A. T. Hagler, P. Damber, J. Am. Chem. Soc. 1979, 101, 5111-5131.
48. R. Fletcher, C. M. Reeves, Comput. J. 1964, 7, 149-154.
49. W. F. van Gunsteren, M. Karplus, J. Comput. Chem. 1980, 1, 266-274.
50. W. F. van Gunsteren, H. J. C. Berendsen, Angew. Chem. 1990, 101, 1020-1051;
51. Angew. Chem. Int. Ed. Engl. 1990, 29, 992-1023.
52. K. Wüthrich, M. Billeter, W. Brown, J. Mol. Biol. 1983, 169, 949-961.
53. C. L. Brooks III, B. Montgomery Pettitt, M. Karplus, Advances in Chemical Physics, Vol. LXXI, Wiley, New York, 1988, Chapter 4, pp. 33-37.