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40 results about "Protein chemistry" patented technology

The Chemistry of Biology: Proteins. Proteins. Proteins are organic compounds that contain the element nitrogen as well as carbon, hydrogen, and oxygen. Proteins are the most diverse group of biologically important substances and are often considered to be the central compound necessary for life.

Pictet-spengler ligation for protein chemical modification

Aldehyde- and ketone-functionalized proteins are promising new substrates for the development of chemically modified biotherapeutics and protein-based materials. Their reactive carbonyl groups are typically conjugated with a-effect nucleophiles, such as substituted hydrazines and alkoxyamines, to generate hydrazones and oximes, respectively. However, the resulting C=N linkages are susceptible to hydrolysis under physiologically relevant conditions, which limits their utility in biological systems. Here we introduce a Pictet-Spengler ligation that is based on the classic Pictet-Spengler reaction of aldehydes and tryptamine nucleophiles. The ligation exploits the bioorthogonal reaction of aldehydes and alkoxyamines to form an intermediate oxyiminium ion; this intermediate undergoes intramolecular C-C bond formation with an indole nucleophile to form an oxacarboline product that is hydrolytically stable. The reaction was utilized for site-specific chemical modification of glyoxal- and formylglycine-functionalized proteins, including an aldehyde-tagged variant of the therapeutic monoclonal antibody Herceptin. In conjunction with techniques for site-specific introduction of aldehydes into proteins, the Pictet-Spengler ligation offers a new means to generate stable bioconjugates for medical and materials applications.
Owner:RGT UNIV OF CALIFORNIA

Method for separating copper proteome by using copper-chelated magnetic beads

The invention discloses a method for separating copper proteome by using copper-chelated magnetic beads, and relates to the technical field of protein chemistry. The method comprises the following steps: taking a biological tissue or cell, after fully grinding with liquid nitrogen, adding protein extracting liquid, and after uniformly mixing, carrying out low-temperature centrifugation, so as to obtain a denatured protein solution; mixing the copper-chelated magnetic beads with the denatured protein solution, and incubating to obtain a magnetic bead protein mixed solution; adding a buffer solution 1 with the volume 1 time of that of the magnetic bead protein mixed solution into the magnetic bead protein mixed solution for suspension, pouring half of the supernate under the external magnetic field, and repeating for 4-5 times to obtain a mixed solution A; adding a buffer solution 2 with the volume 1 time of that of the mixed solution A into the mixed solution A, separating all the specific copper-binding proteins, namely, the copper proteome, and collecting the copper proteome under the external magnetic field. According to the method, the metalloproteome is separated under a denaturing condition by using magnetic bead-IDA, so that the procedures are greatly simplified, and the obtaining efficiency of metalloproteins is improved; a method suitable for separating the metalloproteome from the tissue or cell under the excess heavy metal treatment condition is established.
Owner:HENAN UNIV OF SCI & TECH

Pictet-Spengler ligation for protein chemical modification

Aldehyde- and ketone-functionalized proteins are promising new substrates for the development of chemically modified biotherapeutics and protein-based materials. Their reactive carbonyl groups are typically conjugated with a-effect nucleophiles, such as substituted hydrazines and alkoxyamines, to generate hydrazones and oximes, respectively. However, the resulting C═N linkages are susceptible to hydrolysis under physiologically relevant conditions, which limits their utility in biological systems. Here we introduce a Pictet-Spengler ligation that is based on the classic Pictet-Spengler reaction of aldehydes and tryptamine nucleophiles. The ligation exploits the bioorthogonal reaction of aldehydes and alkoxyamines to form an intermediate oxyiminium ion; this intermediate undergoes intramolecular C—C bond formation with an indole nucleophile to form an oxacarboline product that is hydrolytically stable. The reaction was utilized for site-specific chemical modification of glyoxal- and formylglycine-functionalized proteins, including an aldehyde-tagged variant of the therapeutic monoclonal antibody Herceptin. In conjunction with techniques for site-specific introduction of aldehydes into proteins, the Pictet-Spengler ligation offers a new means to generate stable bioconjugates for medical and materials applications.
Owner:GERAWAN FARMING +1

Method for separating specific metal-binding proteins by using protein denaturation

The invention discloses a method for separating specific metal-binding proteins by using protein denaturation, and relates to the technical field of protein chemistry. The method comprises the following steps: firstly, taking a biological tissue or cell, after fully grinding with liquid nitrogen, adding protein extracting liquid, and after uniformly mixing, carrying out low-temperature centrifugation, so as to obtain a denatured protein solution; replacing Ni in Ni-NTA agarose with Cu, and putting into a chromatographic column; incubating the denatured protein solution with Cu-NTA agarose, so as to ensure that the denatured proteins are fully combined with the Cu-NTA agarose; then under the low-temperature condition, injecting eluant 1, so as to renature the proteins and elute non-specific copper-binding proteins; injecting eluant 2, so as to separate specific copper-binding proteins. According to the method, the copper-binding proteins under the denaturing condition are separated by using agarose-NTA, so that the obtaining efficiency of the copper-binding proteins is greatly improved; a technology suitable for separating the specific metal-binding proteins from the biological tissue or cell under the excess heavy metal treatment condition is established.
Owner:HENAN UNIV OF SCI & TECH

A method for separating specific metal-binding proteins by protein denaturation

The invention discloses a method for separating specific metal-binding proteins by using protein denaturation, and relates to the technical field of protein chemistry. The method comprises the following steps: firstly, taking a biological tissue or cell, after fully grinding with liquid nitrogen, adding protein extracting liquid, and after uniformly mixing, carrying out low-temperature centrifugation, so as to obtain a denatured protein solution; replacing Ni in Ni-NTA agarose with Cu, and putting into a chromatographic column; incubating the denatured protein solution with Cu-NTA agarose, so as to ensure that the denatured proteins are fully combined with the Cu-NTA agarose; then under the low-temperature condition, injecting eluant 1, so as to renature the proteins and elute non-specific copper-binding proteins; injecting eluant 2, so as to separate specific copper-binding proteins. According to the method, the copper-binding proteins under the denaturing condition are separated by using agarose-NTA, so that the obtaining efficiency of the copper-binding proteins is greatly improved; a technology suitable for separating the specific metal-binding proteins from the biological tissue or cell under the excess heavy metal treatment condition is established.
Owner:HENAN UNIV OF SCI & TECH
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