Stabilization of protein structures and protein-protein interactions are critical in the engineering of industrially useful enzymes and in the design of pharmaceutically valuable ligands. Hydrophobic interactions involving phenylalanine residues play crucial roles in protein stability and protein-protein/peptide interactions. To establish
Expression of adenosine receptors of the A1, A2A and A2B type has been examined in the post-mortem frontal cortex and hippocampus in argyrophilic grain disease (AGD), a tauopathy affecting the hippocampus but usually not the frontal cortex, in an attempt
Journal of the American Chemical Society, 125(43), 13046-13051 (2003-10-23)
The capacity for sequential and specific exchange of single peptides from coiled-coil heterotrimers is investigated. Dual hydrophobic-hydrophilic interface systems permit iterative cycles of pH-triggered strand exchange that can specifically replace one, two, or even all three initial trimer components. The
Arodyn (Ac[Phe¹,²,³,Arg⁴,D-Ala⁸]Dyn A(1-11)NH₂) is an acetylated dynorphin A (Dyn A) analog that is a potent and selective κ opioid receptor antagonist (Bennett et al., J Med Chem 2002, 45, 5617), and its analog [NMePhe¹]arodyn shows even higher affinity and selectivity
Journal of the American Chemical Society, 126(44), 14447-14451 (2004-11-04)
The design of an antiparallel coiled-coil 1:1:1 heterotrimer is described. Control of strand orientation results from proper alignment of sterically matched hydrophobic core side chains. Matched core layers position one cyclohexylalanine side chain against two alanine ones. Substitution of three
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