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PubMed1983

Toxic activity of seventeen industrial solvents and halogenated compounds on human lymphocytes cultured in vitro.

Seventeen chemicals (solvents, insecticides and intermediates in the production of textiles and resins) were tested in a short-term in vitro system with human lymphocytes to determine their toxic action. The parameters studied were the tritiated thymidine uptake and cell viability in cultures grown with or without a rat liver metabolizing system (S-9 mix). Data obtained showed that 1,3-dichlorobenzene, 1,2-dichlorobenzene, hexane, 1,2-diiodoethane, 1,4-dichlorobenzene, tetrachloroethylene, 2,3-dibromopropanol, chloromethyl methyl ether, 1,2- and 1,3-dibromopropane, in order, exerted the more toxic effects; ethyl acetate, cyclohexane, cyclohexanone and benzene showed lower toxic activity. The chemicals lost their toxic power in the presence of the metabolizing system with the exception of 1,2- and 1,3-dichlorobenzene which maintained in some degree their toxicity even in the presence of the S-9 mix. Only chloromethyl methyl ether elicited unscheduled DNA synthesis acting as DNA damaging agent.

Adult↗
PubMed1975

Specific detection of volatile metabolites in urines of normal subjects and patients with diabetes mellitus using computerized mass fragmentography.

Volatile urinary components are analyzed by a combination of gas chromatography, mass spectrometry and a data-acquisition system. Mass fragmentograms using the mass spectrometric data on magnetic tape are recorded for the primary aliphatic alcohols ethanol, n-propanol, isobutanol and isopentanol and the ketones 4-hepatonone and cyclohexanone. The mass fragmentograms are used as selective profiles to facilitate recognition of abnormalities in the urinary components in cases of diabetes mellitus.

1-Propanol↗
PubMed1982

[Affinity chromatography of NAD(P)+ dehydrogenases dependent on the concentration of NAD(P)+ bound to ketones or aldehydes].

The use of general ligands such as NAD(P)+ for affinity chromatography of dehydrogenase requires elution with pulses of oxidized or reduced cofactor at suitable concentrations. This method of elution can involve considerable effort before ideal eluent conditions are evolved. We report on a new method of immobilized NAD(P)+ modifications which increases the selectivity of the phase and may be of rather wide application. The immobilized NAD(P)+ is modified by addition of a ketone or an aldehyde substrate of the dehydrogenase which must be purified and becomes a very specific ligand of that dehydrogenase. The adduct of immobilized NAD+ and sodium pyruvate absorbs specifically the lactate dehydrogenase, whereas the adduct of immobilized NAD+ and cyclohexanone adsorbs specifically the horse liver alcohol dehydrogenase. Absorbed dehydrogenases are eluted with NaCl gradients.

Aldehydes↗
PubMed1997

The synthesis of (R)-(+)-lipoic acid using a monooxygenase-catalysed biotransformation as the key step.

2-(2-Acetoxyethyl)cyclohexanone (4) was converted into the lactone (-)-(5) regio- and enantioselectively using 2-oxo-delta 3-4,5,5-trimethylcyclopentenyl acetyl-CoA monooxygenase, an NADPH-dependent Baeyer-Villiger monooxygenase from camphor grown Pseudomonas putida NCIMB 10007. The lactone (-)-(5) was converted into (R)-(+)-lipoic acid in six steps. In contrast cyclopentanone monooxygenase, an NADPH-dependent Baeyer-Villiger monooxygenase from cyclopentanol-grown Pseudomonas sp. NCIMB 9872 selectively oxidized the (S)-enantiomer of the ketone (4) giving better access to optically enriched, naturally occurring lipoic acid.

Biotransformation↗
PubMed1991

Secondary 15N isotope effects on the reactions catalyzed by alcohol and formate dehydrogenases.

Secondary 15N isotope effects at the N-1 position of 3-acetylpyridine adenine dinucleotide have been determined, by using the internal competition technique, for horse liver alcohol dehydrogenase (LADH) with cyclohexanol as a substrate and yeast formate dehydrogenase (FDH) with formate as a substrate. On the basis of less precise previous measurements of these 15N isotope effects, the nicotinamide ring of NAD has been suggested to adopt a boat conformation with carbonium ion character at C-4 during hydride transfer [Cook, P. F., Oppenheimer, N. J. & Cleland, W. W. (1981) Biochemistry 20, 1817]. If this mechanism were valid, as N-1 becomes pyramidal an 15N isotope effect of up to 2-3% would be observed. In the present study the equilibrium 15N isotope effect for the reaction catalyzed by LADH was measured as 1.0042 +/- 0.0007. The kinetic 15N isotope effect for LADH catalysis was 0.9989 +/- 0.0006 for cyclohexanol oxidation and 0.997 +/- 0.002 for cyclohexanone reduction. The kinetic 15N isotope effect for FDH catalysis was 1.004 +/- 0.001. These values suggest that a significant 15N kinetic isotope effect is not associated with hydride transfer for LADH and FDH. Thus, in contrast with the deformation mechanism previously postulated, the pyridine ring of the nucleotide apparently remains planar during these dehydrogenase reactions.

Alcohol Dehydrogenase↗
PubMed1984

Human liver alcohol dehydrogenase isozymes: reduction of aldehydes and ketones.

The class I (alpha, beta 1, gamma 1, and gamma 2), II (pi), and III (chi) isozymes of human liver alcohol dehydrogenase (ADH) were isolated as electrophoretically homogeneous preparations to examine their kinetics of aldehyde and ketone reduction. While the oxidation of a wide variety of alcohols by ADH has been investigated extensively, the reduction of aldehydes and ketones has received much less attention even though the equilibrium favors the latter process. For each isozyme, the Km and kcat values were measured at pH 7.0 with acetaldehyde, pentanal, octanal, benzaldehyde, and cyclohexanone as substrates. Activity could not be detected with succinic semialdehyde and betaine aldehyde for any of the isozymes. The nonenzymatic hydration, oxidation, and aldol condensation of aldehydes in aqueous solutions present serious experimental obstacles in determining the isozymes' kinetic constants. The effects of these reactions on the enzymatic parameters were studied and compensated for. Michaelis constants for all class I and II isozymes vary by more than 8000-fold, from less than 1 microM for beta 1 gamma 1 and beta 1 beta 1 with octanal to 8.3 mM for pi-ADH for acetaldehyde. However, with any given aldehyde, these values vary by less than 40-fold, and the constants are approximately equal to Km values reported previously for the corresponding alcohols. In contrast, Km values for chi-ADH are extremely high and could be determined accurately only for octanal (75 microM).(ABSTRACT TRUNCATED AT 250 WORDS)

Alcohol Dehydrogenase↗
PubMed1988

Stereochemistry and accessibility of prosthetic groups in flavoproteins.

Using 8-demethyl-8-hydroxy-5-deaza-5-carba analogues of the appropriate flavin nucleotides, we determined the stereochemistry of interaction between coenzyme and substrate for several flavoproteins. The enzymes were D-amino acid oxidase, L-lactate oxidase, and D-lactate dehydrogenase, all three of which interact with pyruvate, as well as cyclohexanone monooxygenase and 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase, which were both probed with nicotinamide nucleotides. L-Lactate oxidase and D-lactate dehydrogenase used the si face of the modified flavin ring while the other three enzymes showed re-side specificity. This selection of flavoenzymes includes FAD- and FMN-dependent enzymes, enzymes that follow a carbanion mechanism, and others that have hydride transfer as an integral part of their reaction pathway.

Apoenzymes↗
PubMed1980

Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions.

Primary deuterium equilibrium isotope effects for the reaction of five secondary alcohols with nicotinamide adenine dinucleotide (DPN) to give reduced deuterionicotinamide adenine dinucleotide (DPND) (cyclohexanol-1-d, 1.18; 2-propanol-2-d, 1.175; threo-DL-isocitrate-2-d, 1.168; L-malate-2-d, 1.173; L-lactate-2-d, 1.19) are all approximately 1.18, while for a primary alcohol, ethanol, the value is 1.07, for an amino acid, L-glutamate-2-d, it is 1.14, and for a hemiacetal, glucose-1-d, it is 1.28. In each case deuterium becomes enriched in the alcohol, amino acid, or hemiacetal with respect to DPNH (TPNH). beta-Secondary equilibrium isotope effects for reduction of ketones by DPNH (cyclohexanone-2,2,6,6-d4, 0.82; acetone-d6, 0.78; pyruvate-d3, 0.83; alpha-ketoglutarate-3,3-d2 reduced to glutamate, 0.898; oxaloacetate-3,3-d2, 0.877; oxaloacetate-3R-d, 0.945) give an average value of 0.946/D, with deuterium becoming enriched in the alcohol or amino acid with respect to the ketone. For reduction of acetaldehyde-1-d by DPNH, the observed value of 0.953 includes the equilibrium effect on the hydration equilibrium in addition to that on the reduction, and the calculated values for reduction of the free aldehyde and the hydrate are 0.78 and 1.07. For reduction of benzaldehyde-1-d, which is not hydrated, the observed value was 0.79. The secondary equilibrium isotope effect for conversion of DPN-4-d to DPNH is 0.89, with deuterium becoming enriched in DPNH, and, for conversion of fumarate-2,3-d2 to malate, the value is 0.69, with deuterium becoming enriched in L-malate. The equilibrium isotope effect for reaction of cyclohexanol-1-d with DPN is temperature independent over the range 15-35 degrees C.

Alcohol Oxidoreductases↗
PubMed1996

Complexation of the tissue plasminogen activator protease with benzamidine-type inhibitors: interference by the kringle 2 module.

Well-resolved high-field 1H NMR signals between -0.1 and -0.7 ppm afford convenient probes to monitor the conformational state of the tissue plasminogen activator (tPA) protease, modulated by covalent inhibitor binding or activation cleavage [Hu, C.-K., Kohnert, U., Wilhelm, O., Fischer, S., & Llinas, M. (1994) Biochemistry 33, 11760-11766]. We have investigated recombinant BM 06.022 (a domain-deletion variant mutant from Escherichia coli comprising the kringle 2 and protease modules) and protease constructs of tPA in both single-chain (sc) and two-chain (tc) forms. The two proteins were studied when confronted with the noncovalent (i.e., reversible) active site inhibitors benzamidine and a series of bisbenzamidine derivatives: 2,5-bis(4-amidinobenzylidene)cyclopentanone, 2,6-bis(4-amidinobenzylidene)cyclohexanone, 2,7-bis(4-amidinobenzylidene)cycloheptanone, and 2,8-bis(4-amidino- benzylidene)cyclooctanone. At pH* 4.6, the 1H NMR spectrum is sensitive to complexation of the protease module with the various effectors. The amplitude of the inhibitor-shifted resonances is more pronounced for the tc-protease than for the sc-protease, suggesting that access of inhibitors to the protease catalytic site is facilitated upon conversion to the tc form. The effects detected by the NMR spectrum suggest a biphasic process, involving stronger (primary) and weaker (secondary) bindings to a single protease active site. Binding to the protease module in tc-BM 06.022 essentially generates the same spectral characteristics as detected upon binding to the isolated tc-protease construct. In contrast, a negligible perturbation by the inhibitors is observed on the (sc) BM 06.022. Hence, in the intact BM 06.022 the kringle 2 is structurally coupled to the protease module thus interfering with inhibitor molecules from accessing the protease active site. These domain-domain interactions relax upon conversion to the catalytically active tc form, thus decoupling the kringle 2 from the protease module in BM 06.022 while simultaneously exposing the active site to become accessible to effectors or substrates.

Amino Acid Chloromethyl Ketones↗
PubMed1995

Nonclassical 2,4-diamino-6-(aminomethyl)-5,6,7,8-tetrahydroquinazoline antifolates: synthesis and biological activities.

Twenty 6-substituted 2,4-diaminotetrahydroquinazolines were designed, synthesized, and biologically evaluated as novel nonclassical inhibitors of dihydrofolate reductase (DHFR) from Pneumocystis carinii and Toxoplasma gondii and as antitumor agents. The 6-substituents included substituted anilinomethyls, with alkoxy (OCH3, and OCH2CH3) and halogen (Cl and Br) moieties on the phenyl ring; an indolinomethyl; and 1-naphthylaminomethyls. The compounds were synthesized from a protected key intermediate 2,4-bis(acetamido)-5,6,7, 8-tetrahydroquinazoline-6-carboxaldehyde (26) by reductive amination with the appropriate amine. Compound 26 was obtained via a Diels--Alder reaction of 2-(trimethylsiloxy) -1,3-butadiene with acrolein to afford cyclohexanone-4-carboxaldehyde dimethyl acetal (23) after deprotection of the silyloxy group and protection of the aldehyde in a single step. Cyclocondensation of 23 with dicyandiamide followed by protection of the 2,4-diamino groups and deprotection of the 6-acetal gave 26. The compounds were significantly potent ((7-330) x 10(-9) M) and selective against T. gondii (versus rat liver DHFR). The most selective analogue against T. gondii DHFR was 2,4-diamino-6-[[(2',5'-dimethoxyphenyl) methylamino]methyl]-5,6,7,8-tetrahydroquinazoline (5) which showed exceptionally high inhibitory activity against the growth of T. gondii cells in culture (IC50 = 5.4 x 10(-8) M). Selected analogues were evaluated as inhibitors of the growth of tumor cells in culture. The most active analogues inhibited the growth of tumor cells at GI50 = 10(-8) M.

Animals↗
PubMed1992

Synthesis and antifolate properties of 5,10-ethano-5,10-dideazaaminopterin.

2-Carbomethoxy-4-(p-carbomethoxyphenyl)cyclohexanone was prepared in a four-step process and thermally condensed with 2,4,6-triaminopyrimidine to afford methyl 2,4-diamino-4-deoxy-7-hydroxy-5,10-ethano-5,10-dideazapteroate+ ++. Reduction of the 7-oxo function with borane gave the 7,8-dihydro pterin which was subsequently oxidized to the fully aromatic pteroate ester with dicyanodichlorobenzoquinone. Saponification of the benzoate ester, coupling with diethyl glutamate and final ester hydrolysis afforded the title compound. This novel deazaaminopterin analogue was approximately as potent as methotrexate in vitro in terms of DHFR and L1210 cell growth inhibition. There are indications of diastereomeric differences in the enzyme inhibition measurements. A significant transport advantage over MTX for influx into L1210 cells was observed. The compound was active against the E 0771 murine mammary solid tumor, but further investigation with individual diastereomers is required to define the ED50.

Aminopterin↗
PubMed1989

(6R,6S)-5,8,10-trideaza-5,6,7,8-tetrahydrofolate and 6(R,6S)-5,8,10-trideaza-5,6,7,8-tetrahydropteroyl-L-ornithine as potential antifolates and antitumor agents.

(6R,6S)-5,8,10-Trideaza-5,6,7,8-tetrahydropteroic acid was synthesized in several steps from 4,4-(ethylenedioxy)-cyclohexanone and [4-(tert-butyloxycarbonyl)benzyl]triphenylphosphonium bromide and was elaborated to (6R,6S)-5,8,10-trideaza-5,6,7,8-tetrahydropteroyl-L-glutamic acid and (6R,6S)-5,8,10-trideaza-5,6,7,8-tetrahydropteroyl-L-ornithin e. Compound 1 was found to be a good substrate for partially purified mouse liver folypolyglutamate synthetase (FPGS), with a Michaelis constant (Km = 15 microM) comparable to that reported for the reduced folate substrate (6S)-5,6,7,8-tetrahydropteroyl-L-glutamic acid and for (6R,6S)-5,10-dideaza-5,6,7,8-tetrahydropteroyl-L-glutamic acid (DDATHF). However, in striking contrast to DDATHF, which is potently cytotoxic, 1 failed to inhibit tumor cell growth in culture at concentrations of up to 100 microM. These results suggested that the NH at position 8 of DDATHF is important for cytotoxic activity but not for polyglutamylation. Just as 1 was a good substrate for FPGS, the ornithine analogue 2 proved to be among the more potent competitive inhibitors of this enzyme discovered to date, with a Ki,s of 10 microM. While the binding affinity of 2 was lower than that reported for 5,6,7,8-tetrahydropteroyl-L-ornithine (H4PteOrn), very substantial FPGS inhibition was observed even though N5,N8, and N10 in H4PteOrn were replaced by carbon. Binding to FPGS thus appears to be tolerant of bioisosteric replacements made simultaneously in ring B and the bridge region. Neither 1 nor 2 was active in preventing cell growth in culture at concentrations of up 100 microM. The N delta-hemiphthaloyl derivative of 2, synthesized as a potential prodrug, was also inactive.

Animals↗
PubMed1989

Alterations in the stereochemistry of the kappa-selective opioid agonist U50,488 result in high-affinity sigma ligands.

The synthesis and in vitro sigma receptor activity of the two diastereomers of U50,488 [(+/-)-2], namely, (1R,2S)-(+)- cis-3,4-dichloro-N-methyl-N-[2-(1-pyrrolidinyl)cyclohexyl]benzeneacet ami de [(+)-1] and (1S,2R)-(-)-cis-3,4-dichloro- N-methyl-N-[2-(1-pyrrolidinyl)cyclohexyl]benzeneacetamide [(-)-1], are described. (+)-1 and (-)-1 were synthesized from (+/-)-trans-N-methyl-2-aminocyclohexanol [(+/-)-3]. Pyridinium chlorochromate (PCC) oxidation of the N-t-Boc-protected derivative of (+/-)-3 afforded (+/-)-2-[N- [(tert-butyloxy)carbonyl]-N-methylamino]cyclohexanone [(+/-)-5]. The sequence of enamine formation with pyrrolidine, catalytic reduction, N-deprotection, and optical resolution afforded (1R,2S)-(-)-cis-2-pyrrolidinyl-N-methylcyclohexylamine [(-)-10] and (1S,2R)-(+)-cis-2-pyrrolidinyl-N-methylcyclohexylamine [(+)-10]. The optical purity (greater than 99.5%) of (-)-10 and (+)-10 was determined by HPLC analysis of the diastereomeric ureas formed by reaction with optically pure (R)-alpha-methylbenzyl isocyanate. The absolute configuration of (-)-10 and (+)-10 was determined by single-crystal X-ray diffractometry of the bis-(R)-mandelate salt. Condensation of optically pure (-)-10 and (+)-10 with 3,4-dichlorophenylacetic acid furnished (+)-1 and (-)-1, respectively. Compounds (+)-1, (-)-1, (-)-2, and (+)-2 were compared for their binding affinities at kappa opioid, sigma, D2-dopamine, and phencyclidine (PCP) receptors in competitive binding assays using [3H]bremazocine ([3H]BREM) or [3H]U69,593, [3H]-(+)-3-(3-hydroxyphenyl)-N-(1-propyl)piperidine [[3H]-(+)-3-PPP], or [3H]-1,3-di(o-tolyl)guanidine ([3H]DTG), [3H]-(-)-sulpiride [[3H]-(-)SULP], and [3H]-1- [1-(2-thienyl)cyclohexyl]piperidine ([3H]TCP), respectively. In the systems examined, (-)-2 exhibited the highest affinity for kappa receptors, with a Ki of 44 +/- 8 nM. However, (-)-2 also showed moderate affinity for sigma receptors, with a Ki of 594 +/- 3 nM [[3H]-(+)-3-PPP]. The (1R,2R)-(+)-enantiomer, (+)-2, had low affinity for both kappa and sigma receptors, exhibiting Ki values of 1298 +/- 49 nM at kappa ([3H]BREM) and 1270 +/- 168 nM at sigma [[3H]-(+)-3-PPP]. In contrast, the chiral cis compounds (+)-1 and (-)-1 showed high affinity for sigma receptors and negligible affinity for kappa opioid receptors in the [3H]BREM assay. Compound (-)-1 exhibited a Ki of 81 +/- 13 nM at sigma receptors [[3H]-(+)-3-PPP] and 250 +/- 8 nM ([3H]DTG).(ABSTRACT TRUNCATED AT 400 WORDS)

3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cycloh↗
PubMed1981

Synthesis of spiro[isobenzofuran-1(3H),4'-piperidines] as potential central nervous system agents. 6. Synthesis, 13C NMR, and biological evaluation of cis- and trans-4-amino-3'-arylspiro[cyclohexane-1,1'(3'H)-isobenzofuran] derivatives.

4-(Dimethylamino)- and 4-(methylamino)-3'-arylspiro[cyclohexane-1,1'(3'H)-isobenzofuran] derivatives were prepared as analogues of previously reported 3-arylspiro[isobenzofuran-1(3H),4'-piperidines]. Metalation of benzanilide with n-butyllithium, addition of 4-(dimethylamino)cyclohexanone, and acidification afforded a mixture of cis- and trans-4-(dimethylamino)spiro[cyclohexane-1,1'(3'H)-isobenzofuran]-3'-ones (1a,b), which were separated by fractional crystallization. Addition of aryllithium or aryl Grignard reagents to 1a,b and formic acid reduction afforded cis- and trans-4-(dimethylamino)-3'-arylspiro[cyclohexane-1,1'(3'H)-isobenzofurans] 3a-f, which were converted to secondary amine analogues 5a-e. Tentative stereochemical assignments are based on chemical arguments and are supported by 13C NMR chemical shift data. Marked inhibition of tetrabenazine-induced ptosis is a property of most antidepressants, and significant antitetrabenazine activity is observed for several of these compounds. Optimal antitetrabenazine activity is associated with the cis-3'-phenyl series, and the cis secondary amine 5a is approximately twice as potent as the cis tertiary amine 3a. The various compounds are relatively weak with respect to potentiation of L-5-hydroxytryptophan-induced seizures.

Animals↗
PubMed1979

Syntheses and antiinflammatory actions of 4,5,6,7-tetrahydroindazole-5-carboxylic acids.

A novel series of 1-aryl-4,5,6,7-tetrahydro-1H-indazole-5-carboxylic acids and 2-aryl-4,5,6,7-tetrahydro-2H-indazole-5-carboxylic acids were synthesized via condensation between a phenylhydrazine and a 2-(hydroxymethylene)cyclohexanone-4-carboxylate, and the antiinflammatory activity was determined. In the carrageenan edema test, 1-aryl-4,5,6,7-tetrahydro-1H-indazole-5-carboxylic acids exhibited fairly high antiinflammatory activity. However, the 2-aryl isomers were far less active than the former. The most active compound of the series was 1-phenyl-4,5,6,7-tetrahydro-1H-indazole-5-carboxylic acid, which had an ED50 value of 3.5 mg/kg.

Analgesics↗
PubMed1976

Drugs derived from cannabinoids. 6. Synthesis of cyclic analogues of dimethylheptylpyran.

Two cyclic analogues 8 and 9 of dimethylheptylpyran (DMHP, 1) were synthesized by the Pechmann condensation of the resorcinol 4 with ethyl 4-methyl-2-cyclohexanone-1-carboxylate followed by Grignard addition with MeMgI. In selected pharmacological tests both analogues 8 and 9 were considered inactive compared to DMHP as CNS and cardiovascular agents.

Animals↗
PubMed1975

Prostaglandins and congeners. Synthesis of simplified prostaglandins. Inhibition of gastric acid secretion by 2-(omega-carboxyalkyl)-3-alkylcycloalkanones.

Simplified prostaglandin analogs were prepared and tested for inhibition of gastric acid secretion. An alkyl moiety of 1-8 carbon atoms was substituted for the C-13 to C-20 chain of the PG's. Analog variations included shortened and lengthened acid side chains, beta-oxidation blockage, beta-ketol, Falpha-hydroxyl, and cyclohexanone substitution. Maximal inhibitory activity was obtained with the shorter alkyl moieties.

Animals↗
PubMed1975

Biologically active polycycloalkanes. 1. Antiviral adamantane derivatives.

Convenient methods for the synthesis of 1-substituted 3-adamantyl chlorides and bromides (2), 1-adamantylphenols and -cresols (3), and 1-adamantylacetic (6) as well as 1,3-adamantanediacetic (11) acids are described. Several novel derivatives were synthesized from these key intermediates: adamantylcyclohexanols (4) and -cyclohexanones (5) from adamantylphenols (3), and esters (7,12, and 22), amides (13 and 18), thioamides (9 and 16), amidine (10), nitrile (15), and amines (14 and 17) from 1-adamantanecarboxylic (19) and -acetic (6) acids and 1,3-adamantanediacetic acid (11). Some adamantylpyrimidines (24) and -purines (25 and 26) were also prepared. Antiviral activities of the compounds obtained in this work and a series of new 1-adamantyl alkyl ketones synthesized before, together with those of some known adamantane derivatives, were tested in vitro on monolayer culture of chick ambryo fibroblasts against Newcastle disease virus.

Adamantane↗