Abstract
In previous studies, it was found that paclitaxel-stabilized microtubules (MTs), hollow protein nanotubes comprised of assembled αβ-tubulin heterodimers, spontaneously assemble into bundles above a critical concentration (∼1.5 mM Spermine) of tetravalent spermine (PNAS 2004, 101, 16099). Further, at concentrations of spermine several-fold higher (∼10 mM Spermine), paclitaxel-stabilized MT bundles (BMT) quickly become unstable and undergo a shape transformation to bundles of inverted tubulin tubules (BITT), the outside surface of which corresponds to the inner surface of the BMT tubules (Nature Materials 2014, 13, 195). Here we will report on our current study of protein Tau-microtubule ordering (in an active system) in the absence of paclitaxel and, in particular, the effect of biological cations on microtubule self-assembly using transmission electron microscopy (TEM) and synchrotron small-angle X-ray scattering (SAXS).
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