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Effect of tubulin binding and self-association on the near-ultraviolet circular dichroic spectra of colchicine and analogues.
Chabin, R M; Feliciano, F; Hastie, S B.
Afiliación
  • Chabin RM; Department of Chemistry, State University of New York, Binghamton 13901.
Biochemistry ; 29(7): 1869-75, 1990 Feb 20.
Article en En | MEDLINE | ID: mdl-2331468
Near-UV circular dichroic (CD) spectra of three colchicine analogues that differ at the C-10 position have been obtained in the presence and absence of tubulin. All three colchicine analogues show dramatic alterations in the low-energy near-UV CD band upon tubulin binding that cannot be mimicked by solvent, but in no event does the rotational strength of the CD band decrease to nearly zero as in the case of colchicine [Detrich, H. W., III, Williams, R. C., Jr., Macdonald, T. L., & Puett, D. (1981) Biochemistry 20, 5999-6005]. The effect of self-association of colchicine and one of the C-10 analogues, thiocolchicine, on the near-UV CD band was also investigated. A qualitative similarity was seen between the near-UV CD spectra of colchicine and thiocolchicine dimers and the spectra of these molecules bound to tubulin. These observations support the previous suggestion that ligands bound to the colchicine site on tubulin may be interacting with an aromatic amino acid in the colchicine binding site [Hastie, S. B., & Rava, R. P. (1989) J. Am. Chem. Soc. 110, 6993-7001].
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tubulina (Proteína) / Colchicina Tipo de estudio: Qualitative_research / Risk_factors_studies Límite: Animals Idioma: En Revista: Biochemistry Año: 1990 Tipo del documento: Article Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tubulina (Proteína) / Colchicina Tipo de estudio: Qualitative_research / Risk_factors_studies Límite: Animals Idioma: En Revista: Biochemistry Año: 1990 Tipo del documento: Article Pais de publicación: Estados Unidos