Turn-folding in fluorescent anthracene-substituted cyclopenta[]isoxazoline short peptides.

Cyclopenta[]isoxazoline aminols were used for the synthesis of β-turn mimics. The peptide chain choice ascertained the influence of their structural features on the applicability/reliability/robustness of these scaffolds as β-turn inducers and their limitations. The amino acid selection as well as steric demands can favor or disfavor the structure folding and the correct design of the peptide chains deeply influences the potential use of these nitrosocarbonyl-based compounds as turn-inducers.

The focal adhesion kinase Pyk2 links Ca2+ signalling to Src family kinase activation and protein tyrosine phosphorylation in thrombin-stimulated platelets.

In blood platelets, stimulation of G protein-coupled receptors (GPCRs) by thrombin triggers the activation of Src family kinases (SFKs), resulting in the tyrosine-phosphorylation of multiple substrates, but the mechanism underlying this process is still poorly understood. In the present study, we show that the time-dependent protein-tyrosine phosphorylation triggered by thrombin in human or murine platelets was totally suppressed only upon concomitant chelation of intracellular Ca(2+) and inhibition of SFKs. Thrombin-induced activation of SFKs was regulated by intracellular Ca(2+) and accordingly the Ca(2+) ionophore A23187 was sufficient to stimulate SFKs.