Inhibition of polo-like kinase 1 suppresses microtubule dynamics in MCF-7 cells.

Polo-like kinase 1 (Plk1) is a mitotic serine/threonine kinase implicated in spindle formation and cytokinesis in mammalian cells. Here, purified Plk1 was found to bind to reconstituted microtubules in vitro. Further, Plk1 was found to co-localize with interphase microtubules in MCF-7 cells and to co-immunoprecipitate with polymerized tubulin.

Thalidomide (5HPP-33) suppresses microtubule dynamics and depolymerizes the microtubule network by binding at the vinblastine binding site on tubulin.

Thalidomides were initially thought to be broad-range drugs specifically for curing insomnia and relieving morning sickness in pregnant women. However, its use was discontinued because of a major drawback of causing teratogenicity. In this study, we found that a thalidomide derivative, 5-hydroxy-2-(2,6-diisopropylphenyl)-1H-isoindole-1,3-dione (5HPP-33), inhibited the proliferation of MCF-7 with a half-maximal inhibitory concentration of 4.

Dinuclear Cu(I) complexes of pyridyl-diazadiphosphetidines and aminobis(phosphonite) ligands: synthesis, structural studies and antiproliferative activity towards human cervical, colon carcinoma and breast cancer cells.

The copper(i) complexes containing phosphorus donor ligands such as diazadiphosphetidine, cis-{(o-OCH2C5H4N)P(μ-N(t)Bu)}2 (1) and aminobis(phosphonite), C6H5N{P(OC6H3(OMe-o)(C3H5-p))2}2 (2, PNP), have been synthesized. Treatment of 1 with copper iodide afforded the 1D coordination polymer [{Cu(μ-I)}2{(o-OCH2C5H4N)P(μ-N(t)Bu)}2]n (3). Treatment of 3 with 2,2'-bipyridine (bpy) and 1,10-phenanthroline (phen) produced mixed-ligand complexes [(L)2Cu2{(o-OCH2C5H4N)P(μ-N(t)Bu)}2][I]2 (4 L = bpy; 5 L = phen) in good yields.

CIL-102 binds to tubulin at colchicine binding site and triggers apoptosis in MCF-7 cells by inducing monopolar and multinucleated cells.

A plant dictamine analog, 1-[4-(furo[2,3-b]quinolin-4-ylamino)phenyl]ethanone (CIL-102) has been shown to exert potent anti-tumor activity. In this study, we examined the mode of interaction of CIL-102 with tubulin and unraveled the cellular mechanism responsible for its anti-tumor activity. CIL-102 bound to tubulin at a single site with a dissociation constant ~0.