H-1 Nuclear Magnetic Resonance Spin-Lattice Relaxation, C-13 Magic-Angle-Spinning Nuclear Magnetic Resonance Spectroscopy, Differential Scanning Calorimetry, and X-Ray Diffraction of Two Polymorphs of 2,6-Di-Tert-Butylnaphthalene

Polymorphism, the presence of structurally distinct solid phases of the same chemical species, affords a unique opportunity to evaluate the structural consequences of intermolecular forces. The study of two polymorphs of 2,6-di-tert-butylnaphthalene by single-crystal x-ray diffraction, differential scanning calorimetry (DSC), C-13 magic-angle-spinning (MAS) nuclear magnetic resonance (NMR) spectroscopy, and H-1 NMR spin-lattice relaxation provides a picture of the differences in structure and dynamics in these materials. The subtle differences in structure, observed with x-ray diffraction and chemical shifts, strikingly affect the dynamics, as reflected in the relaxation measurements. We analyze the dynamics in terms of both discrete sums and continuous distributions of Poisson processes

Inhibitors of Unactivated P38 MAP Kinase

Inhibition of the p38 map kinase pathway has been shown to be beneficial in the treatment of inflammatory diseases. The first class of potent p38 kinase inhibitors was the pyridinylimidazole compounds from SKB. Since then several pyridinylimidazole-based compounds have been shown to inhibit activated p38 kinase in vitro and in vivo. We have developed a novel series of pyridinylimidazole-based compounds, which potently inhibit the p38 pathway by binding to unactivated p38 kinase and only weakly inhibiting activated p38 kinase activity in vitro