title: The importance of the phenyl-tropolone 'aS' configuration in colchicine's binding to tubulin.
abstract: Measuring ellipticities of (+/-)-colchicine and (+/-)-deacetamidocolchicine in the presence of tubulin afforded net positive CD bands with maxima at 340 nm resulting from reduction of the negative ellipticities upon binding of (-) enantiomers to the protein. Results of optical studies together with earlier NMR conformational analysis of these molecules substantiate the hypothesis that colchicinoids bind to tubulin with the phenyl-tropolone moiety in the 'aS' configuration. Natural colchicine which binds to tubulin, therefore, should be referred to as (-)-(aS,7S)-colchicine.
authors.affiliation: Laboratory of Analytical Chemistry, NIDDK, National Institutes of Health, Bethesda, MD 20892.
authors.forename: H J
authors.initials: HJ
authors.lastname: Yeh
authors.forename: M
authors.initials: M
authors.lastname: Chrzanowska
authors.forename: A
authors.initials: A
authors.lastname: Brossi
mesh_terms: D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D003078:Colchicine / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D014404:Tubulin / Q000378:metabolism*
chemical_list: D014404:Tubulin; D003078:Colchicine