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Discovery of PH-797804, a highly selective and potent inhibitor of p38 MAP kinase.
An amphipathic alpha-helical decapeptide in phosphatidylcholine is an effective synthetic lung surfactant.
The data demonstrate that a small water-soluble synthetic peptide containing an amphipathic alpha-helical structure combined solely with the major lipid of natural lung surfactant is effective in restoring lung compliance and gas exchange in surfactants-deficient lungs and may be useful in treatment of the respiratory distress syndromes.
Centrally truncated and stabilized porcine neuropeptide Y analogs: design, synthesis, and mouse brain receptor binding.
It is proposed that the central region of pNPY serves a structural role in the peptide and is not involved in direct receptor interaction.
Discovery of N-substituted pyridinones as potent and selective inhibitors of p38 kinase.
Minimal peptide length for interaction of amphipathic alpha-helical peptides with phosphatidylcholine liposomes.
The interactions of a series of amphipathic alpha-helical peptides containing from 6 to 18 amino acid residues with dipalmitoylphosphatidylcholine and DPPC were studied by optical and calorimetric methods and formed small micellar structures, as judged by gel filtration chromatography.
Interaction of hirudin with thrombin: identification of a minimal binding domain of hirudin that inhibits clotting activity.
It is shown that the carboxyl-terminal 10 amino acid residues 56-65 are minimally required for binding to thrombin and inhibition of clotting and associated with a significant conformational change of Thrombin as judged by circular dichroism.
Development of MDL 28,050, a small stable antithrombin agent based on a functional domain of the leech protein, hirudin.
The development of MDL 28,050 and other effective antithrombin agents are outlined through the description of the structure-activity relationships (SAR) for these peptides, which are effective in a variety of in vitro and in vivo models of thrombosis.
Anticoagulant peptides: nature of the interaction of the C-terminal region of hirudin with a noncatalytic binding site on thrombin.
A "kinked" amphipathic alpha-helical structure, which orients all of the residues most critical for activity on one face of the helix, is proposed for anticoagulant activity in hirudin.