87004-78-2Relevant articles and documents
DIHYDROPYRIMIDINE COMPOUNDS AND USES THEREOF IN MEDICINE
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, (2019/05/10)
Provided herein are a dihydropyrimidine compound and use as a medicament, especially application as a medicament used for treating and preventing hepatitis B. Specifically, provided herein is a compound having Formula (I) or (Ia), or a stereisomer, a tautomer, an N-oxide, a solvate, a metabolite, a pharmaceutically acceptable salt or a prodrug thereof, wherein the variables of the formulas are as defined in the specification. Also provided herein is use of the compound having Formula (I) or (Ia), or an enantiomer, a diastereoisomer, a tautomer, a hydrate, a solvate, or a pharmaceutically acceptable salt thereof as a medicament, especially use as a medicament for treating and preventing hepatitis B.
Dihydropyridine compound and application thereof to drugs
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Paragraph 0573; 0580-0582, (2019/05/08)
The invention relates to a dihydropyridine compound and application of the dihydropyridine compound serving as a drug, in particular to application of the dihydropyridine compound serving as a drug for treating and preventing hepatitis B. Specifically, the invention relates to the compound shown as the general formula (I) or (Ia) (please see the specifications for the general formula (I) or (Ia))or stereoisomers, tautomer, a nitrogen oxide, solvate, metabolites and medically acceptable salt of the compound or a prodrug of the compound, wherein all variables are defined in the specification. The invention further relates to application of the compound shown as the general formula (I) or (Ia) or enantiomers, non-enantiomers, the tautomer, hydrates, the solvate or the medically acceptable salt of the compound serving as drugs, in particular to application of the compound or the enantiomers, the non-enantiomers, the tautomer, the hydrates, the solvate or the medically acceptable salt of the compound serving as the drugs for treating and preventing hepatitis B.
Enantiomeric recognition of carboxylic anions by a library of neutral receptors derived from α-amino acids and o-phenylenediamine
Ulatowski, Filip,Jurczak, Janusz
, p. 962 - 968 (2014/08/18)
A library of eight neutral anion receptors consisting of α-amino acid esters attached to o-phenylenediamine by urea groups was synthesized and analysed in terms of capacity for chiral recognition of carboxylates. The NMR titrations revealed that the assoc
COMPOSITIONS AND METHODS FOR CYCLOFRUCTANS AS SEPARATION AGENTS
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Page/Page column 45-49; 59, (2010/12/31)
The present invention relates to derivatized cyclofructan compounds, compositions comprising derivatized cyclofructan compounds, and methods of using compositions comprising derivatized cyclofructan compounds for chromatographic separations of chemical species, including enantiomers. Said compositions may comprise a solid support and/or polymers comprising derivatized cyclofructan compounds.
Substrate specificity of isopenicillin N synthase
Huffman,Gesellchen,Turner,Rothenberger,Osborne,Miller,Chapman,Queener
, p. 1897 - 1914 (2007/10/02)
Highly purified isopenicillin N synthase (IPNS) from two sources (naturally occurring in Penicillium chrysogenum and that expressed in Escherichia coli via a cloned gene derived from Cephalosporium acremonium) have been isolated and utilized in vitro to test synthetic modifications of the natural substrate, (L-α-amino-δ-adipyl)-L-cysteinyl-D-valine (ACV). A very sensitive procedure utilizing the ability of β-lactams to induce the synthesis of β-lactamase was employed to determine whether an ACV analogue could serve as a substrate for IPNS. A wide variety of amino and carboxyl terminal tripeptide substitutions were examined and found to elicit positive β-lactamase induction profiles. However, none of these modifications were found to function as efficiently as a substrate as ACV. One of the β-lactam products which was formed from the reaction of IPNS and the tripeptide analogue was independently synthesized and evaluated for antibacterial activity. Modification of the L-cysteine residue in the second position of ACV resulted in tripeptides that were unable to serve as substrates. Conversion of the D-valine residue in the third position of ACV to an aromatic amino acid or to a highly electronegative residue such as trifluorovaline resulted in elimination of substrate activity and creation of an inhibitor of the enzyme.