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In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5 interaction

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons77733

Beisel,  H. G.
Holak, Tad / NMR Spectroscopy, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77940

Engh,  R. A.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78123

Holak,  T. A.
Holak, Tad / NMR Spectroscopy, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Kamionka, M., Rehm, T., Beisel, H. G., Lang, K., Engh, R. A., & Holak, T. A. (2002). In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5 interaction. Journal of Medicinal Chemistry, 45(26), 5655-5660.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6DA3-8
Zusammenfassung
Recently we have determined the crystal structure of the insulin-like growth factor-I (IGF-I) in complex with the N- terminal domain of the IGF-binding protein-5 (IGFBP-5). Here we report results of computer screening for potential inhibitors of this interaction using the crystal coordinates. From the compounds suggested by in silico screens, successful binders were identified by NMR spectroscopic methods. NMR was also used to map their binding sites and calculate their binding affinities. Small molecular weight compounds (FMOC derivatives) bind to the IGF-I binding site on the IGFBP-5 with micromolar affinities and thus serve as potential starting compounds for the design of more potent inhibitors and therapeutic agents for diseases that are associated with abnormal IGF-I regulation.