Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP1H-NMR spectroscopy |
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| Affiliation: | 1. Istituto di Chimica delle Macromolecole del C.N.R., Milano Italy;2. Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA U.S.A.;3. Physical Chemistry Laboratory, University of Groningen, Groningen The Netherlands;1. Department of Medical Oncology, Georges Francois Leclerc Cancer Centre, Dijon, France;2. Unit of Methodology and Biostatistics, Georges Francois Leclerc Cancer Centre, Dijon, France;3. Platform of Transfer in Biological Oncology, Georges François Leclerc Cancer Center, Dijon, France;4. Department of Biology and Pathology of tumors, Georges Francois Leclerc Cancer Centre, Dijon, France;5. Department of Surgical Oncology, Georges Francois Leclerc Cancer Centre, Dijon, France;6. University of Burgundy-Franche Comté, 21000 Dijon, France;7. INSERM U1231, 21000 Dijon, France;8. Department of Medical Oncology, Institut Jean Godinot, Reims, France;9. Department of Medical Oncology, Institut de Cancérologie de Lorraine, Nancy, France;10. Department of Medical Oncology, Centre François Baclesse, Caen, France;11. Department of Medical Oncology, Centre Antoine Lacassagne, Nice, France;12. Department of Medical Oncology, Centre Eugène Marquis, Rennes, France;13. Department of Medical Oncology, Institut Curie, Centre René Huguenin, Saint-Cloud, France;14. Department of Medical Oncology, Centre Jean Perrin, Clermont-Ferrand, France;1. University of Dayton, Department of Chemistry, USA;2. Murray State University, Department of Chemistry, USA;3. University of Dayton, Department of Mathematics, USA;4. New Mexico Highlands University, Department of Chemistry and Biochemistry, USA |
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| Abstract: | Photo-chemically induced dynamic nuclear polarization (photo-CIDNP) one-dimensional and two-dimensional (2D)1H-NMR techniques have been applied to the study of the kringle 4 domain of human plasminogen both ligand-free and complexed to the antifibrinolytic drugs ɛ-aminocaproic acid and p-benzylaminesulfonic acid (BASA). A number of aromatic side-chains (His3, Trp72, Tyr41, Tyr50 and Tyr74) appear to be exposed and accessible to 3-N-car☐ymethyl-lumiflavin, the photopolarizing flavin dye, both in the presence and in the absence of ligands. A lesser exposure is observed for the Trp25 and Trp62 indole groups in the presence of BASA. The spin-spin (J-coupling) and dipolar (Overhauser) connectivities in the 2D experiments afford absolute assignment of aromatic resonances for the above residues, as well as of those stemming from the Trp72 ring in the presence of BASA. Moreover, a number of Hβ resonances can be identified and sorted according to specific types of amino acid residues. |
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