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 medicinal chemistry, 40(11), 1565-1569 (1997-05-23)
In an effort to prepare orally bioavailable analogs of our previously reported thrombin inhibitor 1, we have synthesized a series of compounds that utilize the unique amino acid D-dicyclohexylalanine as a P3 ligand. The resulting compounds are extremely potent and
Tuning wasp toxin structure for nicotinic receptor antagonism: cyclohexylalanine-containing analogues as potent and voltage-dependent blockers.
Journal of the American Chemical Society, 124(33), 9779-9783 (2002-08-15)
Specific coiled-coil heterotrimers result from steric matching of hydrophobic core side chains. A 2:1 heterotrimer is formed by peptides containing alanine or cyclohexylalanine, respectively, at a central core residue. Detailed thermodynamic analysis reveals that the designed complex is considerably more
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