Jenny M. Wai

3'-Tetrahydrofuranylglycine as a novel, unnatural amino acid surrogate for asparagine in the design of inhibitors of the HIV protease

The blockade of the HIV protease has become a major target in the search for an effective therapy for AIDS.1 While many reports of potent HIV-1 inhibitors have appeared recently, the compound Ro 31-8959 remains the least selective for the HIV-1 and HIV-2 proteases.2 This property may result in reduced susceptibility to resistance since these represent the genetically most divergent strains of HIV presently known to exist.

Amiloride derived inhibitors of acid-sensing ion channel-3 (ASIC3).

A series of amiloride derivatives modified at the 5-position of the pyrazine ring were evaluated as inhibitors of acid-sensing ion channel-3 (ASIC3), a novel target for the treatment of chronic pain.

Novel conformationally constrained HIV-1 protease inhibitors: rational design, enzyme inhibition, and X-ray structure of an enzyme-inhibtor complex

Abstract A new class of conformationally restricted HIV-1 protease inhibitors was designed based upon molecular modeling studies of known hydroxyethylamine (HEA) type inhibitors. The structure activity relationships for this series of compounds are discussed and an X-ray crystal complex between one of the inhibitors, L-707,897 and HIV-1 protease is presented.