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A conformational analysis of a stereochemically complete set of peptide analogues based on a cis-enediol unit is presented. The ability of each of the stereoisomers to mimic natural peptides, evaluated by this method, is correlated with its experimental activity in a renin inhibition assay.

5-(trifluoromethyl)-2'-deoxyuridine 5'-monophosphate (CF3dUMP) inhibits thymidylate synthase (TS) from Lactobacillus casei. In the absence of 5,10-methylenetetrahydrofolate, CF3dUMP binds to the active site of TS and attacks the catalytic nucleophile cysteine 198 to form a covalent complex. Tyrosine 146 and cysteine 198 of the TS are bound covalently to CF3dUMP in the complex.

Thevalidity of the chemically initiated electron exchange luminescence (CIEEL) proposed to explain the bacterial luminescence reaction involving bacterial luciferase was investigated. The study protocol involved the synthesis of various stable 4a,5-dihydroflavin model compounds substituted at the 8-position. The one-electron oxidation potentials of the 4a,5-dihydro forms actas intermediates during catalysis by the flavin-dependent monooxygenase luciferase. The 1-electron oxidation potentials of the model compounds correlated linearly with the corresponding redox potentials, thus supporting the CIEEL.

Examines the conformational analysis of a stereochemical complete set of cis-enediol peptide analogues. Computation of energy surfaces for all dihedral angle values; Ability of stereoisomers to mimic natural peptides; Determination of the energy surfaces of the peptide analogues.

Cyclosporin A is effective in the treatment of asthma patients, but its chronic use is limited by toxicity. Novel cyclosporin A analogues were synthesized utilizing the olefin metathesis reaction and evaluated in a calcineurin A inhibition assay. The novel analogues demonstrated activity comparable to activity of the parent molecule and are potential soft drugs.