Enhanced binding and conformational selectivity in affinity capillary electrophoresis using a water-soluble resorcin[4]arene as intrinsic buffer and electrokinetic host.

Affinity capillary electrophoresis (ACE) is a widely used technique for quantifying non-covalent molecular interactions that is dependent on the specific buffer conditions selected. In this study, dynamic 1:1 host-guest inclusion complexation involving a charged resorcin[4]arene with a group of neutral corticosteroids was examined by ACE, where the macrocycle serves as both an intrinsic buffer and electrokinetic host. It was determined that over a 200% enhancement in the apparent binding constant (KB) was realized by ACE when using the host as an intrinsic buffer at pH 7.

Novel fluoropeptidomimetics: synthesis, stability studies and protease inhibition.

Designer fluoropeptidomimetics as protease inhibitors are revealed. The key peptidomimetic region in the inhibitors contains a '-CHF-S-' moiety and is designed to mimic the tetrahedral oxyanion species during the hydrolysis of a peptide bond. Designed fluoropeptidomimetics in aqueous methanol slowly (in several hours to days) yielded the corresponding methyl ether and/or the oxazole derivatives after cyclization.

Design and synthesis of novel fluoropeptidomimetics as potential mimics of the transition state during peptide hydrolysis.

alpha-Fluoroamino acids were targeted in our ongoing efforts to design novel fluoropeptidomimetics (1) as potential protease inhibitors. alpha-Fluoroglycine derivative (2) and alpha-fluoro-beta-aminoethanethiol derivatives (3-9) were synthesized for the first time en route to obtain the peptidomimetic moiety 1. The stability of 2-9 was investigated under organic as well as aqueous conditions.