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Organic & Biomolecular Chemistry Aug 2015The biofilm state is an integral part of the lifecycle of many bacterial pathogens. Identifying inhibitors as molecular probes against bacterial biofilms has numerous...
The biofilm state is an integral part of the lifecycle of many bacterial pathogens. Identifying inhibitors as molecular probes against bacterial biofilms has numerous potential biomedical applications. Here we report quinoline amino alcohol as a highly potent disruptor of V. cholerae biofilms. Additionally, was able to disperse preformed biofilms, an activity exhibited by few compounds with biofilm inhibiting activity.
Topics: Amino Alcohols; Biofilms; Drug Design; Quinolines; Vibrio cholerae
PubMed: 26156292
DOI: 10.1039/c5ob01134e -
Journal of the American Chemical Society Jul 2020Asymmetric C-H amination via nitrene transfer is a powerful tool to prepare enantioenriched amine precursors from abundant C-H bonds. Herein, we report a regio- and...
Asymmetric C-H amination via nitrene transfer is a powerful tool to prepare enantioenriched amine precursors from abundant C-H bonds. Herein, we report a regio- and enantioselective synthesis of γ-alkynyl γ-aminoalcohols via a silver-catalyzed propargylic C-H amination. The protocol was enabled by a new bis(oxazoline) (BOX) ligand designed via a rapid structure-activity relationship (SAR) analysis. The method utilizes accessible carbamate esters bearing γ-propargylic C-H bonds and furnishes versatile products in good yields and excellent enantioselectivity (90-99% ). The putative Ag-nitrene is proposed to undergo enantiodetermining hydrogen-atom transfer (HAT) during the C-H amination event. Density functional theory calculations shed insight into the origin of enantioselectivity in the HAT step.
Topics: Amination; Amino Alcohols; Catalysis; Density Functional Theory; Ligands; Models, Molecular; Molecular Structure; Silver; Stereoisomerism
PubMed: 32659081
DOI: 10.1021/jacs.0c05726 -
Chemical Research in Toxicology May 2021-Propargylamines are useful synthetic scaffolds for the synthesis of bioactive molecules, and in addition, they possess important pharmacological activities. We obtained...
-Propargylamines are useful synthetic scaffolds for the synthesis of bioactive molecules, and in addition, they possess important pharmacological activities. We obtained several neuroprotective molecules, chiral 1,2-amino alcohols and 1,2-diamines, able to reduce by almost 70% the rotenone and oligomycin A-induced damage in SH-SY5Y cells. Furthermore, some molecules assessed also counteracted the toxicity evoked by the Ser/Thr phosphatase inhibitor okadaic acid. Before extrapolating these data to preclinical studies, we analyze the molecules through an prediction system to detect carcinogenicity risk or other toxic effects. In light of these promising results, these molecules may be considered as a lead family of neuroprotective and relatively safe compounds.
Topics: Amino Alcohols; Cell Line, Tumor; Cell Survival; Humans; Molecular Structure; Morphinans; Neuroprotective Agents
PubMed: 33635058
DOI: 10.1021/acs.chemrestox.0c00519 -
The Biochemical Journal Dec 1953
Topics: Amino Alcohols; Brain; Phosphatidylethanolamines
PubMed: 13115371
DOI: 10.1042/bj0550768 -
The Journal of Biological Chemistry Sep 1953
Topics: Amino Alcohols; Ethanolamine; Ethanolamines
PubMed: 13084608
DOI: No ID Found -
Journal of the American Chemical Society Mar 2020A double functionalization of C-H bonds has been developed, wherein a β amine and γ iodide are incorporated onto an aliphatic alcohol in a single operation. This...
A double functionalization of C-H bonds has been developed, wherein a β amine and γ iodide are incorporated onto an aliphatic alcohol in a single operation. This approach is enabled by an imidate radical chaperone, which selectively affords a transient β alkene that is amino-iodinated in situ. Overall, the radical-polar-crossover cascade entails the following key steps: (i) β C-H iodination via 1,5-hydrogen atom transfer (HAT), (ii) desaturation via I complexation, and (iii) amino-iodination of an in situ generated allyl imidate. The synthetic utility of this double C-H functionalization is illustrated by conversion of aliphatic alcohols to a diverse collection of α,β,γ substituted products bearing heteroatoms on three adjacent carbons. The radical-polar crossover mechanism is supported by various experimental probes, including isotopic labeling, intermediate validation, and kinetic studies.
Topics: Alcohols; Amino Alcohols; Free Radicals; Hydrocarbons, Iodinated; Imines; Molecular Structure
PubMed: 32141741
DOI: 10.1021/jacs.0c01318 -
Bacteriological Reviews Sep 1967
Review
Topics: Amino Alcohols; Candida; Carbohydrates; Extracellular Space; Fatty Acids; Fatty Acids, Nonesterified; Fermentation; Fungi; Glycosides; Hydrocarbons; Lipid Metabolism; Lipids; Microscopy, Electron; Yeasts
PubMed: 4864730
DOI: 10.1128/br.31.3.194-213.1967 -
Proceedings of the Royal Society of... Mar 1973
Review
Topics: Acetanilides; Adrenergic beta-Antagonists; Amino Alcohols; Anxiety; Aversive Therapy; Bicarbonates; Calcium; Chronic Disease; Heart Rate; Humans; Injections, Intravenous; Lactates; Phosphates; Propranolol; Propylamines
PubMed: 4144580
DOI: No ID Found -
The Biochemical Journal Jul 19671. A wide range of intermediary metabolites and substrate analogues have no effect on the oxidation of dl-1-aminopropan-2-ol to aminoacetone by washed-cell suspensions...
1. A wide range of intermediary metabolites and substrate analogues have no effect on the oxidation of dl-1-aminopropan-2-ol to aminoacetone by washed-cell suspensions of Escherichia coli. Only dl-2-hydroxy-2-phenylethylamine, dl-1,3-diaminopropan-2-ol, dl-serine and l-1-(3,4-dihydroxyphenyl)-2-aminoethanol act as inhibitors. 2. Dialysed cell-free extracts of E. coli exhibit an NAD(+)-dependent dl-1-aminopropan-2-ol-dehydrogenase activity of approx. 8mmumoles of aminoacetone formed/mg. of protein/min. at the pH optimum of approx. 10. The K(m) values for the coenzyme and dl-amino alcohol are approx. 0.4 and 10.0mm respectively. A smaller peak of activity occurs at pH7.0-7.2, the K(m) for NAD(+) at pH7 being approx. 0.05mm. 3. Enzyme activity in cell-free extracts is inhibited by dl-2-hydroxy-2-phenylethylamine, dl-1-aminopropane-2,3-diol and dl-serine. dl-Phenylserine and dl-1-aminobutan-2-ol are oxidized to compounds reacting as amino ketones. 4. In fresh cell-free extracts l(+)-1-aminopropan-2-ol preparations are oxidized more rapidly than racemic or laevo-rotatory material, the d(-)-enantiomorph appearing to act as a competitive inhibitor. The K(m) for l(+)-1-aminopropan-2-ol appears to be approx. 1.5mm when highly resolved substrate preparations are used, either in the free base form or as the l(+)-tartrate salt. 5. l(+)-1-Aminopropan-2-ol dehydrogenase is a labile enzyme, and in appropriately treated extracts activity towards the d-enantiomorph is detectable and relatively higher than that towards the l-enantiomorph. 6. Optimum activity of l-threonine-dehydrogenase in cell-free extracts is exhibited at pH9.6 in the presence of NAD(+). The K(m) values for coenzyme and amino acid substrate are approx. 0.08 and 5.0mm respectively. This enzyme is distinct from 1-aminopropan-2-ol dehydrogenases on the basis of kinetic evidence, and the separation of activities by gel filtration. 7. Both l-threonine and dl-1-aminopropan-2-ol dehydrogenases are markedly inhibited by 8-hydroxyquinoline and p-chloromercuribenzoate, but only slightly by other chelating and thiol reagents. 8. E. coli is incapable of growth on simple synthetic media, containing a variety of carbon sources, when dl-1-aminopropan-2-ol is supplied as the sole source of nitrogen. It appears unlikely that the micro-organism can deaminate aminoacetone. 9. The metabolic roles of l-threonine dehydrogenase, aminoacetone and 1-aminopropan-2-ol dehydrogenases are discussed.
Topics: Acetone; Alcohol Oxidoreductases; Alcohols; Amino Acid Oxidoreductases; Amino Alcohols; Arsenicals; Chromatography, Gel; Dinitrophenols; Escherichia coli; Fluorides; Fluoroacetates; Hydrogen-Ion Concentration; Iodoacetates; Ketones; Phenethylamines; Phlorhizin; Threonine
PubMed: 5340733
DOI: 10.1042/bj1040112 -
The Biochemical Journal Sep 1968
Topics: Amino Alcohols; Animals; Carbon Isotopes; Chickens; Choline; Chromatography, Thin Layer; Cytosine Nucleotides; In Vitro Techniques; Lipids; Liver; Microsomes; Mitochondria, Liver; Phosphotransferases; Sphingomyelins
PubMed: 5679375
DOI: 10.1042/bj1090310