Axial hydrophobic fence in highly-stable Ni(II) complex of des-angiotensinogen N-terminal peptide

Journal of the American Chemical Society

Volumn 118, Issue 19, 1996, Pages 4727-4728

  Bal, Wojciech ^a,c   Chmurny, Gwendolyn N ^a   Hilton, Bruce D ^a   Sadler, Peter J ^b   Tucker, Alan ^b  

^a NATIONAL CANCER INSTITUTE   (United States)

^b UNIVERSITY OF LONDON   (United Kingdom)

^c UNIVERSITY OF WROC AW   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

ANGIOTENSINOGEN DERIVATIVE;

ARTICLE; COMPLEX FORMATION; NUCLEAR MAGNETIC RESONANCE; REACTION ANALYSIS; STEREOCHEMISTRY;

EID: 0029952282     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja953988j     Document Type: Article

References (27)

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2. High concentrations of des-angiotensinogen have been reported to occur in some important human conditions, e.g. in patients with elevated plasma renin concentrations secondary to bacterial sepsis: Hilgenfeldt, U. Mol. Cell. Endncrinol. 1988, 56, 91-98.
3. GenPept (Gene Bank Products), database distributed by National Cancer Institute. Frederick Biomedical Supercomputing Center. For Gen-Bank, cf.: Burks, C.; Cassidy, M.; Cinkosky, M. J.; Cumella, K. E.; Gilna, P., Hayden, J. E. D.; Kelley, T. A.: Kelly, M.; Kristofferson, D., Ryals, J. Nucleic Acids Res. 1991, 19 (Suppl.), 2221-2225.
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5. E.g.: (a) Camerman, N.; Camerman, A.; Sarkar, B. Can. J. Chem. 1967, 54, 1309-1316. (b) Bal, W.; Djuran, M. I.; Marserum, D. E.; Gray, E T. Jr., Mazid, M. A., Tom, R. T.; Nieboer, E.; Sadler, P. J. J. Chem. Soc. Chem. Commun. 1994, 1889-1890.
6. E.g.: (a) Camerman, N.; Camerman, A.; Sarkar, B. Can. J. Chem. 1967, 54, 1309-1316. (b) Bal, W.; Djuran, M. I.; Marserum, D. E.; Gray, E T. Jr., Mazid, M. A., Tom, R. T.; Nieboer, E.; Sadler, P. J. J. Chem. Soc. Chem. Commun. 1994, 1889-1890.
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11. Dolovich, J : Evans, S. L.; Nieboer. E Br J. Ind Med 1984, 41, 51-55
12. Bal, W.; Kozlowski, H.; Kupryszewski, G.; Mackiewicz, Z.: Pettit. L.: Rubbins. R. J. Inorg Biochem. 1993, 52, 79-87
13. a values of VIHN were calculated using SUPERQUAD (Gans, P.; Sabatini, A., Vacca, A. J. Chem. Soc., Dalton Trans. 1985, 1195-1199) from pH-metric titration curves obtained using a Molspin automatic titrator. The pH electrode was calibrated in terms of hydrogen ion concentration: Irving, H., Miles, M. G.: Pettit, L. D. Anal. Chim. Acta 1967, 38, 475-488.
14. a values of VIHN were calculated using SUPERQUAD (Gans, P.; Sabatini, A., Vacca, A. J. Chem. Soc., Dalton Trans. 1985, 1195-1199) from pH-metric titration curves obtained using a Molspin automatic titrator. The pH electrode was calibrated in terms of hydrogen ion concentration: Irving, H., Miles, M. G.: Pettit, L. D. Anal. Chim. Acta 1967, 38, 475-488.
15. 4 sites involving a His residue. see e.g., ref 6a, p 407
16. + would be 0.2 log units higher
17. Pettit, G.; Pettit, L. D. IUPAC Stability Constants Database: IUPAC and Academic Software: Leeds, U K., 1993
18. Spectra (500 MHz) were recorded on a Varian VXR500S spectrometer. Transmitter presaturation was used to suppress the residual HOD resonance: the "clean" TOCSY sequence (mixing time 50 ms) was used (Bax, A., Davis, J. J. Magn. Reson. 1985, 65, 355-360. Levitt, M: Freeman, R.; Frenkiel, T. A. J. Magn. Reson. 1982, 47, 328-330), with spin-lock 90° pulse width of 32 μs, with 32 μs delays between pulses The Tr-ROESY sequence used a + 180. -180 spin lock with 90° pulse of 37.5 μs, spectral width 3852 Hz. total recycle time 3.07 s. Peaks are referenced to TSP via internal acetate (1.92 ppm).
19. Spectra (500 MHz) were recorded on a Varian VXR500S spectrometer. Transmitter presaturation was used to suppress the residual HOD resonance: the "clean" TOCSY sequence (mixing time 50 ms) was used (Bax, A., Davis, J. J. Magn. Reson. 1985, 65, 355-360. Levitt, M: Freeman, R.; Frenkiel, T. A. J. Magn. Reson. 1982, 47, 328-330), with spin-lock 90° pulse width of 32 μs, with 32 μs delays between pulses The Tr-ROESY sequence used a + 180. -180 spin lock with 90° pulse of 37.5 μs, spectral width 3852 Hz. total recycle time 3.07 s. Peaks are referenced to TSP via internal acetate (1.92 ppm).
20. Piantini, U., Sorensen, O. W.; Ernst, R. R. J. Am. Chem. Soc. 1982, 104, 6800-6801
21. Hwang, T. L.; Shaka, A. J J Am. Chem. Soc 1992, 114, 3157-3159.
22. Structures were calculated from imerproton distances and dihedral angle constraints (Table S2) using the program X-PLOR version 3.1, by A. T. Brunger, Yale University Press, 1992. Lower distance bounds were van der Waals radii, and upper distance bounds were set as 1.2 times the calculated interproton distances. Dihedral angles were constrained to be within ±30° of the ideal calculated angle. Parameters for Ni(II) were adapted from a force field previously developed for the program CHARMrn, which reproduced known square-planar Ni(II) peptides well (Sadler, P. J.: Tucker, A. Unpublished results ). A square-planar arrangement of the coordinating N atoms was obtained from an initial structure calculation even without the constraint imposed by insertion of a square-planar metal ion.
23. Structures were calculated from imerproton distances and dihedral angle constraints (Table S2) using the program X-PLOR version 3.1, by A. T. Brunger, Yale University Press, 1992. Lower distance bounds were van der Waals radii, and upper distance bounds were set as 1.2 times the calculated interproton distances. Dihedral angles were constrained to be within ±30° of the ideal calculated angle. Parameters for Ni(II) were adapted from a force field previously developed for the program CHARMrn, which reproduced known square-planar Ni(II) peptides well (Sadler, P. J.: Tucker, A. Unpublished results ). A square-planar arrangement of the coordinating N atoms was obtained from an initial structure calculation even without the constraint imposed by insertion of a square-planar metal ion.
24. Figure 1A,B was produced using Setor version 4.13.4: Evans, S. V. J. Mol. Graphics 1993, 11, 134-138.
25. Raysheba, J. M. T.; Magaerum, D. Inorg. Chem. 1980, 19, 837-843.
26. Yamashita, M. M., Wesson, L : Eisenman, G : Eisenberg, D Proc Natl. Acad. Sci. U.S.A. 1990, 87, 5648-5652
27. Regan, L. Annu. Rev. Biophys. Biomol. Struct. 1993, 22, 257-281.