Preparation of site-specific isotopically labelled zervamicins, the antibiotic peptaibols produced by Emericellopsis salmosynnemata

Journal of Peptide Science

Volumn 2, Issue 6, 1996, Pages 341-350

  Egorova Zachernyuk, T A ^a   Shvets, V I ^a   Versluis, K ^b   Heerma, W ^b   Creemers, A F L ^c   Nieuwenhuis, S A M ^c   Lugtenburg, J ^c   Raap, J ^c,d  

^a MIREA RUSSIAN TECHNOLOGICAL UNIVERSITY   (Russian Federation)

^b UTRECHT UNIVERSITY   (Netherlands)

^c LEIDEN UNIVERSITY   (Netherlands)

^d LEIDEN UNIVERSITY   (Netherlands)

Author keywords

Biosynthesis; Deuterium; Ion channel forming peptide; Nitrogen 15; Positive ion FAB mass spectrometry

Indexed keywords

EMERICELLOPSIS SALMOSYNNEMATA;

ANTIINFECTIVE AGENT; DEUTERIUM; ION CHANNEL; NITROGEN; PEPTIDE; ZERVAMICIN IC; ZERVAMICIN IIA; ZERVAMICIN IIB; ZERVAMICIN-IC;

ARTICLE; ASCOMYCETES; BIOSYNTHESIS; ISOLATION AND PURIFICATION; ISOTOPE LABELING; METABOLISM;

ANTI-BACTERIAL AGENTS; DEUTERIUM; HYPOCREALES; ION CHANNELS; ISOTOPE LABELING; NITROGEN ISOTOPES; PEPTIDES;

EID: 0030275699     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.72     Document Type: Article

References (22)

1. E. Benedetti, A. Bavoso, B. Di Blasio, V. Pavone, C. Pedone, C. Toniolo and G. M. Bonora (1982). Peptaibol antibiotics: a study on the helical structure of the 2-9 sequence of emerimicins III and IV. Proc. Natl. Acad. Sci. USA 79, 7951-7954.
2. P. Balaram, K. Krishna, M. Sukumar, I. R. Mellor and M. S. P. Sansom (1992). The properties of ion channels formed by zervamicins. Eur. Biophys. J. 21, 117-128.
3. I. L. Karle, J. L. Flippen-Anderson, S. Agarwalla and P. Balaram (1991). Crystal structure of [Leu-1]zervamicin, a membrane ion-channel peptide: implications for gating mechanisms. Proc. Natl. Acad. Sci. USA 88, 5307-5311.
4. I. L. Karle, J. L. Flippen-Anderson, S. Agarwalla and P. Balaram in Structure & Function, volume 2: Proteins, R. H. Sarma and M. H. Sarma, Eds., p. 97-111, Adenine Press, 1992.
5. I. L. Karle, J. L. Flippen-Anderson, S. Agarwalla, and P. Balaram (1994). Conformation of the flexible bent helix of Leu-1-zervamicin in crystal C and a possible gating action for ion passage. Biopolymers 34, 721-735.
6. S. Agarwalla, I. R. Mellor, M. S. P. Sansom, I. L. Karle, J. L. Flippen-Anderson, K. Uma, K. Krishna, M. Sukumar and P. Balaram (1992). Zervamicins, a structurally characterized peptide model for membrane ion channels. Biochem. Biophys. Res. Commun. 186, 8-15.
7. M. S. P. Sansom, P. Balaram, and I. L. Karle (1993). Ion channel formation by zervamicin-IIB. Eur. Biophys. J. 21, 369-383.
8. J. Lugtenburg, R. A. Mathies, R. G. Griffin and J. Herzfeld (1988). Structure and function of rhodopsins from solid state NMR and resonance Raman spectroscopy of isotopic retinal derivatives. Trends Biochem. Sci. 13, 388-393.
9. 13C NMR rotational resonance determination of the Schiff base configuration in the M photointermediate of bacteriorhodopsin. J. Am. Chem. Soc. 115, 8515-8516.
10. 13C] tyrosines. Biochemistry 31, 11038-11049.
11. B carbonyl groups in Rhodobacter sphaeroides R26 reaction centers. FEBS Lett 370, 88-92.
12. R. A. Kinsey, A. Kintanar and E. Oldfield (1981). Dynamics of amino acid side chains in membrane proteins by high field solid state deuterium nuclear magnetic resonance spectroscopy. J. Biol. Chem. 256, 9028-9036.
13. W. Hu, K.-C. Lee and T. A. Cross (1993). Tryptophans in membrane proteins: indole ring orientation and functional implications in the gramicidin channel. Biochemistry 32, 7035-7047.
14. R. E. Koeppe, J. A. Killian and V. Greathouse (1994). Orientation of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy. Biophys. J. 66, 14-24.
15. F. Separovic, J. Gehrmann, T. Milne, B. A. Cornell, S. Y. Lin and R. Smith (1994). Sodium ion binding in the gramicidin A channel. Solid-state NMR studies of the tryptophan residues. Biophys. J. 67, 1495-1500.
16. A. D. Argoudelis, A. Dietz and L. E. Johnson (1974). Zervamicins I and II, polypeptide antibiotics produced by Emericellopsis salmosynnemata. J. Antibiot. 27, 321-328.
17. A. D. Argoudelis and L. E. Johnson (1975). Antibiotics zervamicin I and zervamicin II and process for preparing the same. US Patent 3,907,990.
18. J. Raap, C. Winkel, A. H. M. de Wit, A. H. H. van Houten, A. J. Hoff and J. Lugtenburg (1990). Mass spectrometric determination of isotopically labelled tyrosines and tryptophans in photosynthetic reaction centers of Rhodobacter sphaeroides R-26. Anal Biochem. 190, 9-15.
19. P. Roepstorff and F. Fohlmann (1984). Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass Spectrom. 11, 601.
20. K. L. Rinehart Jr, L. A. Gaudioso, M. L. Moore, R. C. Pandey, J. C. Cook Jr, M. Barber, R. D. Sedgwick, R. S. Bordoli, A. N. Tyler and B. N. Green (1981). Structures of eleven zervamicin and two emerimicin peptide antibiotics studied by fast atom bombardment mass spectrometry. J. Am. Chem. Soc. 103, 6517-6520.
21. K. L. Rinehart Jr, J. C. Cook Jr, H. Meng, K. L. Olson and R. A. Padney (1977). Mass-spectrometric determination of molecular formulas for membrane-modifying antibiotics. Nature 269, 832-833.
22. K. S. Matthews and S. J. Opella (1977). Selectively deuterated amino acid analogues. Synthesis, incorporation into proteins and NMR properties. Biochim. Biophys. Acta 497, 1-13.