Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity

Journal of Biological Chemistry

Volumn 274, Issue 19, 1999, Pages 13181-13192

  Kondejewski, Leslie H ^a   Jelokhani Niaraki, Masood ^a   Farmer, Susan W ^b   Lix, Bruce ^a   Kay, Cyril M ^a   Sykes, Brian D ^a   Hancock, Robert E W ^b   Hodges, Robert S ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPEPTIDE;

ANTIMICROBIAL ACTIVITY; ARTICLE; DISSOCIATION; ENANTIOMER; HEMOLYSIS; HYDROPHOBICITY; LIPID COMPOSITION; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN SYNTHESIS; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; TARGET CELL;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; CANDIDA ALBICANS; CELL MEMBRANE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; GRAM-POSITIVE BACTERIA; HEMOLYSIS; LIPOPOLYSACCHARIDES; MAGNETIC RESONANCE SPECTROSCOPY; MICROBIAL SENSITIVITY TESTS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES, CYCLIC; PROTEIN CONFORMATION; STEREOISOMERISM; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0033532175     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.19.13181     Document Type: Article

References (43)

1. Travis, J. (1994) Science 264, 360-362
2. Hancock, R. E. W. (1997) Lancet 349, 418-422
3. Hancock, R. E. W., and Lehrer, R. (1998) Trends Biotechnol. 16, 82-88
4. Pathak, N., Salas-Auvert, R., Ruche, G., Janna, M.-H., McCarthy, D., and Harrison, R. G. (1995) Proteins Struct. Fund. Genet. 22, 182-186
5. Izumiya, N., Kato, T., Aoyaga, H., Waki, M., and Kondo, M. (1979) Synthetic Aspects of Biologically Active Cyclic Peptides: Gramicidin S and Tyrocidines, pp. 49-89, Halsted Press, New York
6. Dathe, M., Wieprecht, T., Nikolenko, H., Handel, L., Maloy, W. L., MacDonald, K., Beyermann, M., and Bienert, M. (1997) FEBS Lett. 403, 208-212
7. Blondelle, S. E., and Houghten, R. A. (1992) Biochemistry 31, 12688-12694
8. Oren, Z., Hong, J., and Shai, Y. (1997) J. Biol. Chem. 272, 14643-14649
9. Shai, Y., and Oren, Z. (1996) J. Biol. Chem. 271, 7305-7308
10. Oren, Z., and Shai, Y. (1997) Biochemistry 36, 1826-1835
11. Dathe, M., Shumann, M., Wieprecht, T., Winkler, A., Beyermann, M., Krause, E., Matsuzaki, K., Murase, O., and Bienert, M. (1996) Biochemistry 35, 12612-12622
12. Gause, G. F., and Brazhnikova, M. G. (1944) Nature 154, 703
13. Rackovsky, S., and Scheraga, H. A. (1980) Proc. Natl. Acad. Sci. U. S. A. 77, 6965-6967
14. Hull, S. E., Karlsson, R., Main, P., and Woolfson, M. M. (1978) Nature 275, 206-207
15. Ovchinnikov, Y. A., and Ivanov, V. T. (1975) Tetrahedron 31, 2177-2209
16. Kondejewski, L. H., Farmer, S. W., Wishart, D. S., Hancock, R. E. W., and Hodges, R. S. (1996) Int. J. Peptide Protein Res. 47, 460-466
17. Katayama, T., Nakao, K., Akamatsu, M., Ueno, T., and Fumita, T. (1994) J. Pharmacol. Sci. 83, 1357-1362
18. Tamaki, M., Takimoto, M., Nozaki, S., and Muramatsu, I. (1987) J. Chrom. Biomed. Appl. 413, 287-292
19. Kondejewski, L. H., Farmer, S. W., Wishart, D. S., Kay, C. M., Hancock, R. E. W., and Hodges, R. S. (1996) J. Biol. Chem. 271, 25261-25268
20. Gibbs, A. C., Kondejewski, L. H., Gronwald, W., Nip, A. M., Hodges, R. S., and Wishart, D. S. (1998) Nat. Struct. Biol. 5, 284-288
21. Wishart, D. S., Kondejewski, L. H., Semchuk, P. D., Sykes, B. D., and Hodges, R. S. (1996) Letters Peptide Sci. 3, 53-60
22. Wishart, D. S., Sykes, B. D., and Richards, F. M. (1992) Biochemistry 31, 1647-1651
23. Creighton, T. E. (1984) Proteins, pp. 171-237, W. H. Freeman and Company, New York
24. Dauber-Ogusthorpe, P., Roberts, V. A., Ogusthorpe, D. J., Wolff, J., Genest, M., and Hagler, A. T. (1988) Proteins Struct. Funct. Genet. 4, 31-37
25. Eisenberg, D., Schwarz, E., Komaromy, M., and Wall, R. (1984) J. Mol. Biol. 179, 125-142
26. Woody, R. W. (1995) Methods Enzymol. 246, 34-71
27. Sonnichsen, F. D., Van Eyk, J. E., Hodges, R. S., and Sykes, B. D. (1992) Biochemistry 31, 8790-8798
28. Blanco, F. J., Jimenez, M. A., Pineda, A., Rico, M., Santoro. J., and Nietol, J. L. (1994) Biochemistry 33, 6004-6014
29. Cagas, P. M., and Corden, J. L. (1995) Proteins Struct. Funct. Genet. 21, 141-160
30. Parker, J. M. R., Guo, D., and Hodges, R. S. (1986) Biochemistry 26, 5425-5432
31. Guo, D., Mant, C. T., Taneja, A. K., Parker, J. M. R., and Hodges, R. S. (1986) J. Chromotogr. 359, 499-517
32. Zhou, N. E., Mant, C. T., and Hodges, R. S. (1990) Peptide Res. 3, 8-20
33. Rothemund, S., Krause, E., Beyermann, M., Dathe, M., Bienert, M., Hodges, R. S., Sykes, B. D., and Sonnichsen, F. D. (1996) Peptide Res. 9, 79-87
34. Krause, E., Beyermann, M., Fabian, H., Dathe, M., Rothemund, S., and Bienert, M. (1996) Int. J. Peptide Protein Res. 48, 559-668
35. Monera, O. D., Sereda, T. J., Zhou, N. E., Kay, C. M., and Hodges, R. S. (1995) J. Peptide Sci. 1, 319-329
36. Sereda, T. J., Mant, C. T., Sonnichsen, F. D., and Hodges, R. S. (1994) J. Chromatogr. 676, 139-153
37. Hancock, R. E. W. (1981) Antimicrob. Chemother. 8, 429-445
38. Nicas, T. I., and Hancock, R. E. W. (1983) J. Gen. Microbiol. 129, 509-517
39. Moore, R. A., Bates, N. C., and Hancock, R. E. W. (1986) Antimicrob. Agents Chemother. 29, 496-500
40. Loh, B., Grant, C., and Hancock, R. E. W. (1984) Antimicrob. Agents Chemother. 26, 546-551
41. Mant, C. T., Litowski, J. R, and Hodges, R. S. (1998) J. Chromatogr. 816, 65-78
42. Wieprecht, T., Dathe, M., Beyermann, M., Krause, E., Maloy, W. L., MacDonald, D. L., and Bienert, M. (1997) Biochemistry 36, 6124-6132
43. Prenner, E. J., Lewis, R. N. A. H., Neuman, K. C., Gruner, S. M., Kondejewski, L. H., Hodges, R. S., and McElhaney, R. N. (1997) Biochemistry 36, 7906-7916