Distances between the paclitaxel, colchicine, and exchangeable GTP binding sites on tubulin.

Distances between the paclitaxel, colchicine, and exchangeable GTP binding sites on tubulin polymers have been probed using fluorescence spectroscopy. Techniques for measuring fluorescence resonance energy transfer (FRET) between fluorescent or chromophoric ligands for each binding site were employed. 2-Debenzoyl-2-(m-aminobenzoyl)paclitaxel (2-AB-PT) was the fluorophore ligand for the paclitaxel binding site; thiocolchicine, allocolchicine, and MDL 27048 were probes for the colchicine site, and 2'(or 3')-O-(trinitrophenyl)guanosine 5'-triphosphate (TNP-GTP) was the fluorophore ligand for the exchangeable GTP site.

Interaction of a fluorescent derivative of paclitaxel (Taxol) with microtubules and tubulin-colchicine.

A fluorescent derivative of paclitaxel, 2-debenzoyl-2-(m-aminobenzoyl)paclitaxel (2-AB-PT), has been prepared. 2-AB-PT induces microtubule assembly in vitro, but is about 3-fold less potent than paclitaxel itself. The absorption and emission characteristics of 2-AB-PT were analyzed as a function of solvent.

Vacuum ultraviolet circular dichroism of gellan-family polymer films from water and dimethyl sulfoxide.

The denaturing effect of dimethyl sulfoxide (Me2SO) on the conformation of the gellan-welan-rhamsan family of microbial polysaccharides is directly demonstrated by circular dichroism (CD). The three polysaccharides display strikingly similar CD spectra (140-210 nm) for films cast from Me2SO. The disrupting effect of Me2SO on gellan and welan conformations has previously been reported by others on the basis of light-scattering and viscosity studies.