NMR characterization of I19L peptide interacting with tubulin

Marie-Jeanne Clement, Isabelle Jourdain, Sylvie Lachkar, Philippe Savarin, Benoit Gigant, Marcel Knossow, Flavio Toma, Andre Sobel & Patrick Curmi
In the present study, we demonstrate that such peptides derived from stathmin family proteins function as potent autonomous inhibitors of tubulin assembly. The NMR structural study of I19L, the most efficient of these peptides, revealed that, while the free peptide has no preferred conformation, it adopts in solution a beta-hairpin structure upon interaction with tubulin, close to that observed in tubulin-SLD crystals by X-ray analysis. Saturation transfer difference NMR (STD-NMR) spectroscopy allowed us to identify...