4,4-Disubstituted cyclohexylamine based CCR5 chemokine receptor antagonists as anti-HIV-1 agents.

A series of 4,4-disubstituted cyclohexylamine based CCR5 antagonists has been designed and synthesized. Their antiviral structure-activity relationship has been extensively explored.

Frequency-swept HSQC sequences for high-throughput NMR analysis.

This article describes new versions of the DEPT phase-edited heteronuclear single quantum correlation (HSQC) pulse sequence with sensitivity enhancement. The sequences incorporate frequency-swept carbon and proton pulses. The new experiments are inherently robust, well-suited for a high-throughput setting in which sample-to-sample variations may be ignored.

Frequency-swept HMQC sequences for high-throughput NMR analysis.

We describe here new versions of the DEPT phase-encoded HMQC experiment that offer robust performance and improved sensitivity. The new sequences rely on frequency-swept proton and carbon pulses to minimize signal losses from miscalibrated pulses while providing 'J compensation' to optimize the signal strength over a range of heteronuclear coupling constants. By including both proton and carbon-swept pulses, the new sequences also offer an additional signal gain of roughly 10% over well-calibrated hard-pulse experiments.

Relating the structure, activity, and physical properties of ultrashort-acting benzodiazepine receptor agonists.

The ultrashort-acting benzodiazepine (USA BZD) agonists reported previously have been structurally modified to improve aqueous solubility. Lactam-to-amidine modifications, replacement of the C5-haloaryl ring, and annulation of heterocycles are presented. These analogues retain BZD receptor potency and full agonism profiles.

Identification and structure-activity studies of novel ultrashort-acting benzodiazepine receptor agonists.

The synthesis and evaluation of novel ultrashort-acting benzodiazepine (USA BZD) agonists is described. A BZD scaffold was modified by incorporation of amino acids and derivatives. The propionate side chain of glutamic acid tethers an enzymatically labile functionality where the metabolite carboxylic acid displays markedly reduced BZD receptor affinity.