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Buey et al. (p 117) found that the natural product and microtubule stabilizing agent cyclostreptin binds covalently to microtubules first at an exposed site on the microtubule surface and then, upon passing through microtubule pores, at the paclitaxel binding site on the less accessible inner wall. Cyclostreptin effectively arrests the cell cycle in a multidrug-resistant tumor cell line. With the widespread use of microtubule stabilizing agents in cancer chemotherapy, such an irreversible agent has the potential to overcome the resistance characteristic of conventional antimitotic treatments because it can escape ejection from the cell by P-glycoprotein efflux pumps (see also News & Views by Snyder, p 81). Cover art by Erin Boyle, based on images provided by Isabel Barasoain, Oriol Pineda and Fernando Díaz.
The aging of the professoriate has raised questions about how to support productive faculty members late in their careers while integrating the vitality of youthful scientists.
Model systems have evolved with the times, making use of modern biological methods and incorporating biological complexity. This evolution has increased the relevance of models as tools for studying biology.
The nascent field of glycomics is currently undergoing rapid development, largely as a result of advances in technologies for analyzing glycan structure, unraveling glycan-protein interactions and establishing the functional significance of glycans. A meeting was held in November 2006 to explore the challenges and opportunities ahead for this emerging 'omics' domain.
By highlighting the central importance of molecules in life and technology, Molecular Frontiers seeks to increase the interest of young people in science and to identify the potential roles of chemistry and other molecular sciences in addressing global challenges.
Cyclostreptin, a natural product, cell toxin and covalent modifier of microtubules, has been shown to bind irreversibly to a previously unidentified site on the outer wall of microtubules. The exterior low-affinity location seems to be a way-station for microtubule-stabilizing agents traveling to the high-affinity site in the microtubule interior.
Short peptide segments are increasingly found to have critical roles in biological processes but are often difficult to discover. Bioactive peptides can be quickly found through computational approaches, including a new method that has identified several peptides active against platelet function.
Pharmacological chaperones are small molecules that interact with a protein to enhance folding and stability. Understanding the chemistry underlying the interaction of pharmacological chaperones with their target proteins will facilitate the design of more efficient drugs with greater therapeutic potential.
The iron(II)- and 2-oxoglutarate-dependent oxygenases catalyze varied oxidative reactions. Spectroscopic analyses on the catalytic cycle of the chlorinating enzyme CytC3 reveal the presence of chloride–iron(IV)–oxo complexes, expanding the scope of chemistry known to be catalyzed by non-heme iron-oxo species.
The tubulysins inhibit tubulin polymerization, which makes them potent antiproliferative agents and promising lead candidates for the development of new anticancer drugs. The first total synthesis of the most potent member of the tubulysin family, tubulysin D, has been accomplished in a highly convergent manner using an innovative synthetic strategy.
The bacterial transcriptional repressor 6S RNA mimics the DNA contained in a melted promoter and forms specific interactions with the active site of RNA polymerase. A new study shows that, surprisingly, 6S RNA acts as a template for the synthesis of small RNAs, which liberates the polymerase from 6S RNA. Hence, the transcriptional repressor 6S RNA serves as a template for the synthesis of its own de-repressive RNA.