The disruption of the human immunolobulin E-high affinity receptor I (IgE-FcεRI) protein-protein interaction (PPI) is a validated strategy for the development of anti asthma therapeutics. Here, we describe the synthesis of an array of conformationally constrained cyclic peptides based on an epitope of the A-B loop within the Cε3 domain of IgE. The peptides contain various tolan (i.e., 1,2-biarylethyne) amino acids and their fully and partially hydrogenated congeners as conformational constraints. Modest antagonist activity (IC(50) ∼660 μM) is displayed by the peptide containing a 2,2'-tolan, which is the one predicted by molecular modeling to best mimic the conformation of the native A-B loop epitope in IgE.
Stereocontrolled Formation of Styrenes by Pd(0)-Catalyzed Cross-Coupling of Photoactivated (E)-Alkenylgermanes with Aryl Bromides. -The use of PCy3.HBF4 instead of P(o-tolyl)3 gives higher (E)-selectivity, cf. the reaction of the compound (Ia) with the compound (IIf). The germanes (I) bear a fluorous tag to facilitate purification by fluorous solid-phase extraction. -(TSENG, C.-C.; LI, M.; MO, B.; WARREN, S. A.; SPIVEY*, A. C.; Chem. Lett. 40 (2011) 9, 995-997, http://dx.
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