Zastosowanie spektroskopii jądrowego rezonansu magnetycznego w badaniach oddziaływań międzycząsteczkowych ligandów organicznych i biocząsteczek

• Autorzy: Bocian W. , Kozerski L.

Warianty tytułu

EN

Application of nuclear magnetic resonance to study intermolecular interactions of organic ligands and biomolecules

• Języki publikacji: PL

Abstrakty

EN

The title problem is reviewed in the three main areas of general interest to chemists, biochemists and biologists, i.e. mutual interactions of small molecules, ligand to biomolecule binding and interactions of biomolecules. Physical phenomena, specific and nonspecific, such as hydrogen bonding, self association, hydrophobic interactions, etc., are shown as being defined by NMR spectral parameters in solution and solid state. Diversity of hydrogen bonding encountered in nature is exemplified by the interaction of acetic acid with Watson-Crick vs Hoogsteen faces of adenosine, studied by DNMR in organic solvent at low temperatures. The complementarity of solid state NMR to solution studies of defining the nature of hydrogen bonding is presented in the case of genistein interaction with nitrogen bases. Application of a title method is presented for searching the geometry of complexes formed of organic ligands and biological molecules. General protocol for searching the geometry of complex is presented for the case of topotecan (TPT) interaction with duplex octamer and nicked decamer duplexes of DNA. Interaction of biomolecules is presented for the case of duplex octamer DNMR study showing effects of base pairing and stacking on the b 'H values and insulin aggregation as studied by Pulse Field Gradient NMR spectroscopy leading to relating the radius of molecular aggregate with the diffusion constants. In conclusion it is stated that various NMR techniques in solid and liquid state, coupled with X-ray and MS, constitute modern tool of structural biology in pursue of disclosing functions of biomolecules expressed by their interactions.

Słowa kluczowe

PL

oddziaływanie międzycząsteczkowe; biocząsteczki; ligandy organiczne; leki; spektroskopia NMR

EN

intermolecular interaction; biomolecules; organic ligands; drugs; NMR spectroscopy

• Wydawca: Polskie Towarzystwo Chemiczne
• Czasopismo: Wiadomości Chemiczne
• Rocznik: 2005
• Tom: [Z] 59, 1-2
• Strony: 3--22
• Opis fizyczny: Bibliogr. 37 poz.., wykr.

Twórcy

autor

Bocian W.

• Narodowy Instytut Zdrowia Publicznego, ul. Chełmska 30/34, 00-725 Warszawa

autor

Kozerski L.

• Narodowy Instytut Zdrowia Publicznego, ul. Chełmska 30/34, 00-725 Warszawa
• Instytut Chemii Organicznej, Polska Akademia Nauk, ul. Kasprzaka 44/52, 01-224 Warszawa

Bibliografia

• [1] D. Fabris, C. Fenselau, Anal.Chem., 1999, 71, 384.
• [2] L. Kozerski, Org. Magn. Reson., 1982, 20, 194.
• [3] E.M. Basilio Janke, H.-H. Limbach, K. Weisz, J. Am. Chem. Soc.. 2004, 126, 2135.
• [4] L. Kozerski, B. Kamieński, R. Kawęcki, Z Urbańczyk-Lipkowska, W. Bocian, E. Bednarek, J. Sitkowski, K. Zakrzewska, K.T. Nielsen, P.E Hansen, Org. Biomol. Chem., 2003,1, 3578.
• [5] a) K. Polkowski, A.P. Mazurek, Acta Polon. Pharm. Drug Res., 1994, 57, 135; b) P. Fiedor, L. Kozerski, J.Cz. Dobrowolski, R. Kawęcki, K. Biniecki, J. Pachecka, W. Rowiński, A.P. Mazurek, Transplantation Proceedings, 1998,30, 357; c) A.P. Mazurek, K. Biniecki, L. Kozerski, US Patent, 1997, 5, 637, 703; d) F.M. Uckun, W.E. Evans, C.J. Forsyth, K.G. Waddick, L.T. Ahlgren, L.M. Chelstrom, A. Burkhardt, J. Bolen, D.E. Myers. Science, 1995, 267, 886; e) R.A Dixon, D. Ferreira, Phytochemistry; 2002, 60, 205; f) T. Akiyama, J. Ishida, S. Nakagawa, H. Ogawara, S. Watanabe, N. Itoh, M. Shibuya, Y. Fukami, J. Biol. Chem., 1987, 262, 5592; g) J. Markovits, S. Junqua, F. Goldwasser, A-M. Venuat, C. Luccioni, J. Beaumatin, J.-M. Saucier, A. Bernheim, A.J. Sablon, Biochem. Pharmacology, 1995, 50, 177; h) A. Constantinou, K. Kiguchi, E. Huberman, Cancer Res., 1990, 50, 2618; i) P.S. Fiedor, M. Maksymowicz, K. Biniecki, L. Kozerski, R. Kawęcki, J.Cz. Dobrowolski, J. Pachecka, P. Aranjo, W. Rowiński, A. P. Mazurek, Congress of European Society for Artificial Organs, Warsaw, October 17-19, 1996 (Abstract no. 196) p. 3.
• [6] M. Breton, G. Precigoux, Ch. Courseille, M. Hospital, Acta Crystallogr. Sect. B: Struct. Crystallogr. Cryst. Chem., 1975,31, 921.
• [7] A.P. Mazurek, L. Kozerski, J. Sadlej, R. Kawęcki, E. Bednarek, J. Sitkowski, J.Cz. Dobrowolski, J.K. Maurin, K. Biniecki. J. Witowska, P. Fiedor, J. Pachecka, J. Chem. Soc. Perkin 2, 1998, 1223
• [8] M.S. Searle, Progress in NMR Spectroscopy, 1993,25,403.
• [9] a) H.-J. Schneider, F. Hacket, V. Rudiger, H. Ikeda, Chem. Rev., 1998,98, 1755; b) S S. Wijmenga, M. Kruithof. C.W. Hilbers. J. Biomol. NMR, 1997,10,337.
• [10] a) A.N. Lane, Methods Enzymol., 2001, 340, 252; b) M.A. Keniry, R.H. Shafer, Methods Enzymol., 1995, 261, 575.
• [11] a) J.-Sh. Chen, R.B. Shirts, J. Phys. Chem., 1985, 89, 1643; b) H.K.S. Tan, J. Chem. Soc. Faraday Trans, 1994, 90, 3521; c) L. Fielding, Tetrahedron, 2000, 56, 6151.
• [12] a) A. Gafni, Y. Cohen, J. Org. Chem., 1997, 62,120; b) O. Mayzel, Y. Cohen, J Chem. Soc., Chem. Commun., 1994, 1901.
• [13] KA. Connors, Binding Constants, J. Wiley & Sons, New York 1987, rozdz. 4.
• [14] D. Neuhaus. M.P. Williamson, The Nuclear Overhaitser Effect in Structural and Conformational Analysis, VCH Publishers, New York 1989, s. 1.
• [15] M. Zweckstetter, A. Bax, J. Biomol. NMR, 2001, 20, 365.
• [16] K. Lindorff-Larsen, S. Kristjansdittir, K. Teilum, W. Fieber, Ch.M. Dobson, F.M. Poulsen, M. Vendruscolo, J. Am. Chem. Soc., 2004, 126, 3291.
• [17] W. Bocian, R. Kawęcki, E. Bednarek, J. Sitkowski, A Pietrzyk, M. P. Williamson, P.E. Hansen, L. Kozerski, Chem. Eur. J., 2004, 10, 5776.
• [18] W. Bocian, R. Kawęcki. E. Bednarek, J. Sitkowski, M.P. Williamson, P.E. Hansen, L. Kozerski, praca w przygotowaniu.
• [19] M.P. Williamson, T. Asakura, J. Magn. Reson. Series B, 1993,101, 63.
• [20] N.J. Baxter, M.P. Williamson, T.H. Lilley, E. Haslam, J. Chem. Soc., Faraday Trans. 1996, 92,231.
• [21] A.R. Waldeck, P.W. Kuchel, A.J. Lennon, B.E. Chapman, Progr. Nucl. Magn. Reson. Spectrosc., 1997.30, 39.
• [22] B.J. Stockman, C. Dalvit, Progr. Nucl. Magn. Reson. Spectrosc., 2002, 41, 187
• [23] A.H.-J. Wang, Curr. Opin. Struct. Biol., 1992, 2. 361.
• [24] E.R.P. Zuiderweg, Biochemistry, 2002, 41, 1.
• [25] S. Spera, A. Bax. J. Am. Chem. Soc., 1991, 113, 5490.
• [26] D.S. Wishart, C.G. Bigam, A Holm, R.S. Hodges, B.D. Sykes, J. Biomol. NMR 1995, 5, 67.
• [27] M. Lin, C. Larive, Anal. Biochem., 1995, 229,214.
• [28] C.S. Johnson, J. Magn. Reson., 1993, A102,214.
• [29] E.J. Cabrita, S. Beiger, P. Brauer, J. Karger, J. Magn. Reson., 2002,157, 124.
• [30] R.Z-T. Luo, D.R. Beniac, A Fernandez, C.C. Yip, F.P. Ottensmeyer, Science, 1999, 285, 1077.
• [31] Q.-X. Hua, S.N. Gozani, R.E. Chance, J.A. Hoffman, B.C. Frank, M.A Weiss, Nat. Struct. Biol, 1995,2, 129.
• [32] X. Chang, M.M. Jorgensen, P. Bardrum, J. J. Led, Biochemistry, 1997, 36, 9409.
• [33] D. Keller, R. Clausen, K. Josefsen, J.J. Led, Biochemistry, 2001, 40, 10732.
• [34] R. Cahill Jr, Diabetes. 1971, 20, 785.
• [35] H. Hernandez, C.V. Robinson, J. Biol. Chem., 2001, 276, 46685.
• [36] E.J. Nettelton, P. Tito, M. Sunde, M. Bouchard, Ch.M. Dobson, C.V. Robinson, Biophys. J., 2000, 79, 1053.
• [37] J.A. Loo, Mass Spectrometry Rev., 1997,16, 1.