- Methods for producing nylon 7
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Nylon 7 may be produced from biomass derived 6-carbon hydroxymethyl furan compounds as the raw material. The hydroxymethyl furan compounds may be homologated to form an aldehyde that may be aminated to produce an amino carbonyl compound. Hydrogenation/hydro-deoxygenation of the amino-carbonyl compound provides nylon 7.
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- MATERIALS AND METHODS OF PRODUCING 7-CARBON MONOMERS
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This document describes materials and methods for producing 7-hydroxyheptanoic acid using a β-ketothiolase or a synthase and an alcohol O-acetyltransferase to form a 7-acetyloxy-3-oxoheptanoyl-CoA intermediate. This document describes biochemical pathways for producing 7-hydroxyheptanoic acid using a β-ketothiolase or a synthase and an alcohol O-acetyltransferase to form a 7-acetyloxy-3-oxoheptanoyl-CoA intermediate. 7-hydroxyheptanoic acid can be enzymatically converted to pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine or 1,7 heptanediol. This document also describes recombinant hosts producing 7-hydroxyheptanoic acid as well as pimelic acid, 7-aminoheptanoic acid, heptamethylenediamine and 1,7 heptanediol.
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Page/Page column 51; 52
(2016/07/27)
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- HISTONE DEACETYLASE 6 SELECTIVE INHIBITORS FOR THE TREATMENT OF BONE DISEASE
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This invention relates to methods for treating bone disease associated with osteoclast activation using HDAC6 selective inhibitors, e.g., small molecule inhibitors such as reverse amide compounds.
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Page/Page column 72
(2013/03/26)
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- REVERSE AMIDE COMPOUNDS AS PROTEIN DEACETYLASE INHIBITORS AND METHODS OF USE THEREOF
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The present invention relates to novel "reverse amide" compounds comprising a zinc chelator group, and the use of such compounds in the inhibition of HDAC6 and in the treatment of various diseases, disorders or conditions related to HDAC6.
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Page/Page column 76-78
(2011/08/08)
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- Comparison of N-terminal modifications on neurotensin(8-13) analogues correlates peptidestability but not binding affinity with in vivo efficacy
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Neurotensin(8-13) and two related analogues were used as model systems to directly compare various N-terminal peptide modifications representing both commonly used and novel capping groups. Each N-terminal modification prevented aminopeptidase cleavage but surprisingly differed in its ability to inhibit cleavage at other sites, a phenomenon attributed to long-range conformational effects. None of the capping groups were inherently detrimental to human neurotensin receptor 1 (hNTR1) binding affinity or receptor agonism. Although the most stable peptides exhibited the lowest binding affinities and were the least potent receptor agonists, they produced the largest in vivo effects. Of the parameters studied only stability significantly correlated with in vivo efficacy, demonstrating that a reduction in binding affinity at NTR1 can be countered by increased in vivo stability.
- Orwig, Kevin S.,Lassetter, McKensie R.,Hadden, M. Kyle,Dix, Thomas A.
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supporting information; experimental part
p. 1803 - 1813
(2009/12/30)
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- Synthesis of ω-nitro acids and ω-amino acids by ring cleavage of α- nitrocycloalkanones
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The reaction of various α-nitrocycloalkanones 1 with aqueous 0.05 M NaOH, at 80 °C, in the presence of cetyltrimethylammonium chloride (CTACl) as a cationic surfactant, produces ω-nitro acids 2 in good yields. Reduction of the latter with HCOONH4/Pd-C, in methanol, at 80 °C affords ω-amino acids 3. The synthesis of methyl 9-oxodecanoate (8) is also reported.
- Ballini, Roberto,Papa, Fabrizio,Abate, Corrado
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- Lactams in sulfuric acid. The mechanism of amide hydrolysis in weak to moderately strong aqueous mineral acid media
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Reaction rate constants obtained in moderately concentrated sulfuric acid for the hydrolysis of simple lactams of ring sizes five, six, seven, and eight as a function of acidity and temperature have been analyzed using the excess acidity kinetic method. The basicity constants for these substrates have been recalculated; the 13C NMR spectra used to obtain these values are very sensitive to medium effects. It was found that the basicities of the lactams at 0.003-0.1 M lactam concentration were over half a pK unit more basic than they were at 0.5 M lactam, presumably because of the medium effect. Apart from this, the rate constant results obtained at different times by different groups using different techniques for monitoring the kinetics are in adequate agreement. The excess acidity analysis showed that the kinetics could be fitted according to the 'three-water-molecule followed by one-water-molecule' mechanistic scenario previously found, or could just as well be fitted by a 'one-water-molecule followed by unknown mechanism' scenario, with the mechanistic change taking place at 50 wt.% sulfuric acid for all the substrates. Other evidence makes the latter seem the more likely possibility of the two, and activation parameters based upon the 'one-water- molecule' process were determined. Sufficient data points to enable the unknown mechanism to be established were not present; possible mechanisms applicable in media more concentrated than 50 wt.% sulfuric acid are discussed. Previously obtained values of the parameter r, the number of water molecules involved with the substrate in A2 processes, are now questionable.
- Cox, Robin A.
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p. 649 - 656
(2007/10/03)
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- Asymmetric synthesis of non-natural homologues of lysine
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A series of non-natural amino acid homologues of L- and D-lysine have been synthesized and protected for use in solid-phase peptide synthesis. With these residues, electrostatics and hydrophobicity of peptides can be enhanced or altered.
- Kennedy, Kevin J.,Lundquist IV, Joseph T.,Simandan, Tiberiu L.,Beeson, Craig C.,Dix, Thomas A.
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p. 1937 - 1940
(2007/10/03)
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- Synthesis and Physicochemical Properties of Schiff Bases of Amino Acids with Salicylaldehyde
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A series of the Schiff bases of α- and ω-amino acids with salicylaldehyde was synthesized.The physicochemical properties of the substances obtained, including the fluorescent characteristics, were examined, and the hydrolysis constants at pH 6.0, 7.0, and 8.0 were determined.Key words: amino acids, hydroxybenzaldehyde, Schiff bases, fluorescence, hydrolysis constant
- Lurie, E. Yu.,Mosina, E. M.,Efremova, A. A.,Kaplun, A. P.,Shvets, V. I.
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p. 520 - 523
(2007/10/03)
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