64 results about "Enzyme Interaction" patented technology

Methods, products, and kits for identifying an analyte in a sample are provided. One embodiment of a method for identifying an analyte in a sample includes combining the sample with a first reactant capable of specifically coupling to the analyte. The first reactant is coupled to beads. The method also includes combining additional reactant with the beads. The additional reactant is capable of specifically coupling to the analyte or a second reactant coupled to an analyte. An enzyme is attached to the additional reactant. In addition, the method includes combining a substrate with the beads. The substrate is capable of specifically interacting with the enzyme to form a modified substrate. If the substrate interacts with the enzyme attached to the beads via the additional reactant, the solubility of the substrate changes causing the modified substrate to bind to a surface of the beads and / or the reactants bound to the beads. The method further includes identifying the analyte in the sample by detecting the modified substrate bound to the surface of the beads and / or the reactants bound to the beads.

The present disclosure provides pharmaceutical compositions, and their methods of use, where the pharmaceutical compositions comprise a prodrug that provides enzymatically-controlled release of a drug and an enzyme inhibitor that interacts with the enzyme(s) that mediates the enzymatically-controlled release of the drug from the prodrug so as to attenuate enzymatic cleavage of the prodrug. The disclosure provides pharmaceutical compositions which comprise an enzyme inhibitor and a prodrug that contains an enzyme-cleavable moiety that, when cleaved, facilitates release of the drug.

The embodiments provide prodrug compounds of Formulae I-XV. The present disclosure also provides compositions, and their methods of use, where the compositions comprise a prodrug compound of Formulae I-XV that provides controlled release of an opioid. Such compositions can optionally provide a trypsin inhibitor that interacts with the enzyme that mediates the controlled release of an opioid from the prodrug so as to attenuate enzymatic cleavage of the prodrug.

Methods are provided for manipulating nucleic acid to produce gene fusions, to delete or clone a portion of a chromosome, or to insert a sequence into a chromosome. The methods employ sequential transposition processes using two or more pairs of inverted repeat transposase-interacting sequences on a transposable polynucleotide wherein each pair of transposase-interacting sequences interacts with a distinct transposase enzyme.

Pharmaceutical compositions and their methods of use are provided, where the pharmaceutical compositions comprise a phenol-modified opioid prodrug that provides enzymatically-controlled release of a phenolic opioid, and an enzyme inhibitor that interacts with the enzyme(s) that mediates the enzymatically-controlled release of the phenolic opioid from the phenol-modified opioid prodrug so as to modify enzymatic cleavage of the phenol-modified opioid prodrug.

Pharmaceutical compositions and their methods of use are provided, where the pharmaceutical compositions comprise a phenolic opioid prodrug that provides enzymatically-controlled release of a phenolic opioid, and an enzyme inhibitor that interacts with the enzyme(s) that mediates the enzymatically-controlled release of the phenolic opioid from the prodrug so as to attenuate enzymatic cleavage of the prodrug.

Systems and methods are provided for immobilizing nucleic acid amplicons and protein antigens on a test device. Amplicons comprising a synthetic binding unit and a detectable label are generated and immobilized at predetermined locations on a test device by specific binding interactions between the synthetic binding unit and a synthetic capture unit located at the predetermined locations. The synthetic binding unit may include a unique design such that during amplification, a region of the synthetic binding unit is not subject to the amplification reaction, and thus the amplicon remains single stranded and available for binding to the synthetic capture unit during the capture process. In certain embodiments, the synthetic binding unit and a synthetic capture unit include synthetic nucleic acid analogs that do not interact with native nucleic acids or enzymes that act thereon. In one embodiment the synthetic binding unit and synthetic capture unit comprises puranosyl RNA (pRNA).

Pharmaceutical compositions and their methods of use are provided, where the pharmaceutical compositions comprise an opioid prodrug that provides enzymatically-controlled release of an opioid, and an enzyme inhibitor that interacts with the enzyme(s) that mediates the enzymatically-controlled release of the opioid from the opioid prodrug so as to attenuate enzymatic cleavage of the opioid prodrug.

The embodiments provide prodrug compounds of Formulae I-XVII. The present disclosure also provides compositions, and their methods of use, where the compositions comprise a prodrug compound of Formulae I-XVII that provides controlled release of an active agent. Such compositions can optionally provide a trypsin inhibitor that interacts with the enzyme that mediates the controlled release of an active agent from the prodrug so as to attenuate enzymatic cleavage of the prodrug.

The embodiments provide prodrug compounds of Formulae I-XVII. The present disclosure also provides compositions, and their methods of use, where the compositions comprise a prodrug compound of Formulae I-XVII that provides controlled release of an active agent. Such compositions can optionally provide a trypsin inhibitor that interacts with the enzyme that mediates the controlled release of an active agent from the prodrug so as to attenuate enzymatic cleavage of the prodrug.

Pharmaceutical compositions and their methods of use are provided, where the pharmaceutical compositions comprise a phenolic opioid prodrug that provides enzymatically-controlled release of a phenolic opioid, and an enzyme inhibitor that interacts with the enzyme(s) that mediates the enzymatically-controlled release of the phenolic opioid from the prodrug so as to attenuate enzymatic cleavage of the prodrug.

Antimicrobial compositions for oral delivery, and administration to the colon, distal ileum, or other portion of the gastrointestinal tract other than the stomach, of bacteriophage, phage proteins, antimicrobial peptides, or antimicrobial aptamers, are disclosed. In one embodiment, the active agent is capable of lysing the bacterial cell wall. In another embodiment, the active agent is capable of interacting with a receptor or enzyme in the bacteria. In some embodiments, the active agents selectively act on one or more harmful bacteria, such as Clostridium difficile, and either do not act, or act to a lesser extent, on helpful bacteria, such as bifidobacteria. When the agents are not delivered directly to the colon, they active agents ultimately enter the colon and affect the bacteria that are present in the colon. The compositions can include beads of pectin in the form of a cationic salt enclosing the active agent, or other types of drug delivery systems designed for targeted delivery to the desired portion of the gastrointestinal tract.

The present invention relates to methods for the characterization of enzymes or of enzyme-compound complexes, wherein the enzyme is obtained from a protein preparation with the help of at least one broad spectrum ligand immobilized on a solid support and wherein the enzyme is characterized by mass spectrometry. These methods are useful for the screening of non-immobilized compound libraries, selectivity profiling of lead compounds and mechanism of action studies in living cells.

Pharmaceutical compositions and their methods of use are provided, where the pharmaceutical compositions comprise an amphetamine prodrug that provides enzymatically-controlled release of amphetamine or an amphetamine analog. The composition can further comprise an enzyme inhibitor that interacts with the enzyme(s) that mediates the enzymatically-controlled release of amphetamine or the amphetamine analog from the amphetamine prodrug so as to attenuate enzymatic cleavage of the amphetamine prodrug.

The present disclosure provides pharmaceutical compositions, and their methods of use, where the pharmaceutical compositions comprise a prodrug that provides enzymatically-controlled release of a drug and an enzyme inhibitor that interacts with the enzyme(s) that mediates the enzymatically-controlled release of the drug from the prodrug so as to attenuate enzymatic cleavage of the prodrug. The disclosure provides pharmaceutical compositions which comprise an enzyme inhibitor and a prodrug that contains an enzyme-cleavable moiety that, when cleaved, facilitates release of the drug.

A method of providing a patient with controlled release of ketone-containing opioid using a prodrug capable, upon enzymatic activation and intramolecular cyclization, of releasing the ketone-containing opioid is disclosed. The disclosure also provides such prodrug compounds and pharmaceutical compositions comprising such compounds. Such pharmaceutical compositions can optionally include an enzyme inhibitor that interacts with the enzyme(s) to mediate the enzymatically-controlled release of the ketone-containing opioid from the prodrug so as to modify enzymatic cleavage of the prodrug. Also included are methods to use such compounds and pharmaceutical compositions.

The present invention relates to screening methods that make use of a histone deacetylase interacting with a myosin phosphatase for the identification of novel therapeutics useful for inhibiting or inducing apoptosis and for the treatment of pathological conditions, such as smooth muscle cell disorder, cardiac hypertrophy or asthma. Also disclosed are methods for inhibiting or inducing apoptosis and for treatment of a pathological condition by administering to a mammal a therapeutically effective amount of a compound that inhibits or increases the dephosphorylation of a histone deacetylase by a myosin phosphatase or inhibits or increases the binding of a histone deacetylase to a myosin phosphatase.

The embodiments provide Compound PC-5, [2-((S)-2-malonylamino-6-amino-hexanoyl amino)-ethyl]-ethyl-carbamic acid hydromorphone ester, or acceptable salts, solvates, and hydrates thereof. The present disclosure also provides pharmaceutical compositions, and their methods of use, where the pharmaceutical compositions comprise a prodrug, Compound PC-5, that provides enzymatically-controlled release of hydromorphone, and, optionally, a trypsin inhibitor that interacts with the enzyme that mediates the enzymatically-controlled release of hydromorphone from the prodrug so as to attenuate enzymatic cleavage of the prodrug.

The invention relates to a method for quantitatively analyzing interaction region and strength of small molecules and protein kinases based on stable isotope labeling and mass spectrometry. Lysine residue stable isotope labeling differential labeling is carried out on protein kinases with and without incubation small molecules, and after equal mass mixing, a protein kinase sample is subjected to enzymolysis and is detected by liquid chromatography-mass spectrometry. The specific region and strength of the interaction between the small molecules and the protein kinases are judged according to the quantitative ratio of the stable isotope labeling of the enzymolysis peptide fragment. The method is quick, simple, stable and efficient, and provides an effective means for researching the interaction region and strength of the small molecules and the protein kinases.

The present invention relates to compounds having the general formula: [Poly]—[(L)z—[R—CHO]]y wherein [Poly] is a water-soluble, non-peptidic polymer component, L is an optionally present linking group, and RCHO is a substrate capable of interacting with one or more protease enzymes to reversibly inhibit said enzyme, and wherein said substrate comprises a peptide or peptide-like aldehyde. The index z is 0 when linking groups are absent and z is 1 when linking groups are present. The index y is at least 1. The inhibitors of the present invention are suitable for use in personal care compositions, inter alia, body washes, shampoos, and skin creams.

The embodiments provide prodrug compounds of Formulae I-XV. The present disclosure also provides compositions, and their methods of use, where the compositions comprise a prodrug compound of Formulae I-XV that provides controlled release of an opioid. Such compositions can optionally provide a trypsin inhibitor that interacts with the enzyme that mediates the controlled release of an opioid from the prodrug so as to attenuate enzymatic cleavage of the prodrug.

The invention relates to a method for detecting hydroquinone on the basis of magnetic quantum dots. The magnetic quantum dots are prepared, and hydroquinone standard solutions with a series of concentrations are prepared; fluorescence intensity before and after a reaction between a product obtained after interaction between the hydroquinone standard solutions and enzyme and the magnetic quantum dots is tested, and a standard curve is established; a change value of the fluorescence intensity before and after a reaction between a product obtained after interaction of a to-be-tested sample and enzyme and the magnetic quantum dots is tested and contrasted with the standard curve, and the content of hydroquinone in the to-be-tested sample is obtained. A magnetic nano-particle and fluorescent quantum dot combined material is used as a fluorescent probe, and the product obtained after interaction of hydroquinone and enzyme serves as a fluorescence quenching agent; compared with an existing hydroquinone detection method, the method has the advantages of high response speed, simplicity and convenience in operation, low cost, high sensitivity and the like; meanwhile, the magnetic quantum dots with superparamagnetism can be recovered and used repeatedly, the detection cost can be effectively reduced, besides, discharge of the quantum dots into the environment can be avoided, and the detection method is environment-friendly.

The present invention relates to compositions and methods for the modulation of both ubiquitin and ubiquitin-like protein mediated modification and degradation of target proteins that includes the steps of contacting the compound with an Ubiquitin-like protein E2 enzyme and an E1 enzyme containing an ISG15 protein and an E1 containing ubiquitin and detecting the effect of the compound on the interaction between the Ubiquitin-like protein E2 enzyme and these two E1 enzymes, and the steps of contacting the compound with an Ubiquitin-like E2 enzyme containing an ISG15 protein or the same E2 enzyme containing ubiquitin and the E3 enymes that function with this E2 enzyme and detecting the effect of the compound on the interaction between these E2 and E3 enzymes.