40 results about "Protein chemistry" patented technology

The present invention concerns a novel means by which chemical preparations can be made. Reactions can be accelerated on special chips using microwave energy. The chips contain materials that efficiently absorb microwave energy causing chemical reaction rate increases. The invention is important in many small scale chemical transformations including those used in protein chemistry and in combinatorial chemistry.

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.

A new and versatile class of cyclic diazodicarboxamides that reacts efficiently and selectively with phenols and the phenolic side chain of tyrosine through an Ene-like reaction is reported. This mild aqueous tyrosine ligation reaction works over a broad pH range and expands the repertoire of aqueous chemistries available for small molecule, peptide, and protein modification. The tyrosine ligation reactions are shown to be compatible with the labeling of native enzymes and antibodies in buffered aqueous solution. This reaction provides a novel synthetic approach to bispecific antibodies. This reaction will find broad utility in peptide and protein chemistry and in the chemistry of phenol-containing compounds.

The invention relates to the fields of protein chemistry, biology and medicine. More specifically, it relates to the design and preparation of proteinmimics of members of the cystine-knot growth factor superfamily. Further, the invention relates to the use of these proteinmimics as a medicament or prophylactic agent. The invention provides proteinmimics of members of the cystine-knot growth factor superfamily, preferably for use in immunogenic and / or therapeutic compositions.

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.

The invention relates to a chemical cross-linking agent for proteins and a preparation method thereof. The multifunctional cross-linking agent provided by the invention has excellent water-solubilityand stability, and high cross-linking efficiency, especially high cross-linking efficiency to arginine, and the multifunctional cross-linking agent is the first extensively-used specific cross-linkingagent for arginine. It is proved that the cross-linking agent has arginine selectivity; and cross-linking reactions of the multifunctional cross-linking agent with proteins of eight modes and oligomeric yeast protein compounds prove the validity of conjugation between the cross-linking agent and arginine. Combined chemical cross-linking and mass spectrometric technology is an effective and rapidly developing technology in structural chemistry and can be effectively applied to analysis of large active protein compounds without strict purification. Due to diversified structural characteristicsof the cross-linking agent, the cross-linking agent presents complementary reactivity, and arginine residues cross-linkable with the cross-linking agent are all specific.

The present invention is related to the field of protein chemistry. In particular, mixed buffer compositions are formulated that allow an accurate identification of agent-induced changes in protein melting point temperatures. Such buffer compositions provide for methods that determine the specific effects of exogenous agents on protein stability, cryoprotective effects and / or protein quality control (e.g., synthesis and / or extraction purity validations).

The invention belongs to the technical field of protein and its function research, in particular to a protein chemical cross-linking agent and its preparation method and application. The structure of the protein chemical cross-linking agent is shown in general formula I. The protein chemical cross-linking agent described in the present invention has the advantages of rapid reaction and no hydrolysis, and it exhibits high-efficiency cross-linking activity when applied to CXMS technology, and can realize specific recognition for arginine and lysine. The cross-linking reactions of protein chemical cross-linking agents of the present invention with six model proteins, ten protein mixtures, multi-subunit yeast protein complexes, 70S ribosomes and exosomes demonstrate that these cross-linking agents bind to lysine The effectiveness of the existing cross-linking agent is not abundant, and the existing succinimide ester cross-linking agent has many problems in the actual process of CXMS technology, such as easy hydrolysis, low selectivity and relatively slow cross-linking reaction. Wait for the question.

The invention provides a method for modifying a hydrazone-linked polypeptide or protein without adding a catalyst, the method comprising the following steps: under the condition of an aqueous buffer, using an electron-deficient benzaldehyde compound represented by formula III as the hydrophilic The electroreagent uses the hydrazide of the polypeptide or protein shown in the formula II as a nucleophile to carry out the hydrazone linking reaction to obtain a hydrazone linking product having the structure shown in the general formula I, wherein, in the formula III, R is a variable structure Substituents, for example, methyl groups, fluorescent molecule substituents, drug molecule substituents, etc. The present invention also provides the electron-deficient benzaldehyde compound of formula III and the polypeptide or protein modified by the electron-deficient benzaldehyde compound obtained by the hydrazone linking polypeptide or protein modification method.

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.