120 results about "Protein surface" patented technology

Disclosed is a method for enhancing the effect of a protein modulator on a protein by modifying the protein modulator so that the protein modulator binds with the surface of the protein, along with a method for modulating a protein's biological function by contacting the protein with such a modified protein modulator. Also described are modified protein modulators having the formula PM-SP-(LK)_p-MCG-(M)_q, where PM is a protein modulator which interacts with an active site or allosteric site of a protein; SP is a spacer; LK is a linker; p is 0 or 1; q is an integer greater than or equal to one; MCG is a metal chelating group; and M is a metal ion.

Disclosed herein are fire-fighting compositions, and methods thereof, comprising a surfactant and a fraction of a fermentation mixture comprised of yeast exoproteins, where the proteins enhance ability of water to extinguish Class A, Class B and Class K fires, as defined by the National Fire Protection Association. In one embodiment the surfactant is optimized to wet and penetrate into the substrate, for example wood, as in a Class A fire. In a second embodiment, the surfactant is optimized for foaming to provide fire fighting protection in a Class B fire. Further embodiments include methods for using the same protein-surfactant fire fighting composition for both polar (e.g., alcohol) and non-polar combustible liquids. In yet another embodiment, methods are described where the proteins comprise stress shock proteins and where the residual protein-surfactant combination that is not degraded from the fire acts to stimulate resident bacterial populations to accelerate the biodegradation of residual hydrocarbons and surfactants from the composition. In another embodiment, the compositions are free of solvents, fluorine-free as in fluoro surfactants and fluoro-polymers.

Using a novel water-soluble, active ester amide-containing functionalized controlled radical polymerization initiator, stimuli responsive polymers have been grown from the surface of a protein, exemplified by chymotrypsin or any protein having surface amino acids that will covalently bind to the active ester amide-containing functionalized initiator. It is shown that changes in temperature or pH can change the conformation of the polymer surrounding the enzyme, which in turn enabled the rational tailoring of enzyme activity and stability. This method has afforded an increase in the activity and stability of the enzyme by an order of magnitude at pH's where the enzyme is usually inactive or unstable. Multimodal temperature responsive protein-block copolymer conjugates are described.

The invention relates to a polyethylene glycol modified protein separating and purifying method. The invention discloses a novel cation chromatography media MacroCap Sp which can induct protein surface charge distribution relation sensitively. The more positive charge on a protein surface, the stronger combination capability of the protein with the MacroCap Sp, and the higher ion gradient is needed for elution. By utilizing the above property, polyethylene glycol modified protein molecule can be effectively separated. The method comprises the following steps: (1) after modification of object protein by polyethylene glycol with active reaction group, adjusting pH value of a reaction solution, wherein the pH value should be lower than isoelectric point of the polyethylene glycol modified protein; (2) loading the reaction solution to balanced MacroCap Sp cation exchange columns; (3) adding a sodium salt solution to carry out ion gradient elution based on a balanced buffer solution, and collecting object peak. The method of the present invention is suitable for effective separation of recombinant human granulocyte stimulating factor modified by the polyethylene glycol and exenatide.

The present invention relates to methods and systems for representing and scoring the similarity of two protein by iteratively rotating and translating one protein surface representation relative to the other protein surface representation in order to maximize (or minimize) a score that represents both the volume between the two surface representations and the similarity in the identities and positions of the residues comprising the two protein surfaces. In another aspect of the invention, such methods and systems are used to compare and annotate a protein comprising a putative functional site of unknown function with a database of reference proteins of known function.

The invention relates to a manufacturing method of protein modified fiber in acrylic fiber surface ingrafted bean juice, which is characterized by comprising the following steps: (1) firstly, putting acrylic fiber into alkaline aqueous solution at certain bath ratio, certain mass ratio density and temperature, and hydrolyzing for a certain time; (2) cleaning and drying to obtain hydrolyzed fiber, and causing the hydrolyzed fiber to react with thionyl chloride to obtain chlorination fiber; and (3) putting the chlorination fiber into the bean juice to be ingrafted into fiber of which the surface is covered with a bean juice protein layer. The invention utilizes the ingrafted and modified method of protein on the acrylic fiber surface in the bean juice to realize protein surface modified efficacy of the acrylic fiber in the bean juice, and the human body affinity, hygroscopicity and antistatic property of fiber can be improved. The method of the invention is simple and feasible, can realize industrial production only by simple fiber aftertreatment equipment and has the characteristics of small production investment, low production cost and the like.

A method for modification of solid substrates with proteins for efficient surface preconcentration of an analyte from multi-component samples before the detection based on desorption-ionization mass spectrometry and immunochemical assays. The claimed subject is a method of modification of surfaces used as substrates for desorption-ionization mass spectrometry and immuno-chemical assays. The method is based on electronebulization (electrospraying) of protein solution, depending on the intended application either enzymes, lectins, or antibodies. The formed charged electrospray is dried in real time by its passing through an evaporation compartment and the resulting beam of desolvated ions impacts onto the surface and binds to it firmly. Such modified surface can be then used for a selective interaction with an affinity partner of the deposited protein, its preconcentration or enzymatic modification followed by an analysis by means of desorption-ionization mass spectrometry or immunochemical assays.

The invention relates to a method for preparing protein-based surfactant by opening protein disulfide linkage. The method is characterized by converting disulfide linkage into sulfonic group by oxidizing disulfide bond in protein of peroxide, and opening the folded coiling structure of the protein to represent the surface activity properties so as to prepare the protein-based surfactant which has the functions of emulsification, foaming, defoaming, washing, decontamination, soakage, and the like; by introducing polar group or nonpolar group into a protein side chain with opened disulfide bond, the surface activity properties of peptide fragments can be further improved or increased; moreover, by adopting treatments including acetylization, succinylation, acylation or phosphorylation, protein surface activity properties such as surface tension, emulsification, foaming, defoaming, washing, decontamination and soakage can be changed further. The method furthest prevents protein polar group and nonpolar group from being damaged, and maintains the structural integrity and property naturalness of protein molecules, thereby converting the protein into natural high-performance surfactant.

The present invention relates to a recombinant self-assembled protein comprising a target-oriented peptide and a use thereof. The recombinant self-assembled protein according to the present invention, comprising a target-oriented peptide, does not require an additional process for providing target-orientedness, and is thus capable of delivering a desired drug to a target tissue or target cell without using additives, such as chemical binders or stabilizers; therefore, the protein can be used for photothermal therapy, drug delivery, imaging, or the like. In particular, according to the present invention, it is to possible to prepare gold-protein nanoparticle fusions in which uniform high-density gold nanoparticles having target-orientedness are bound to protein surfaces, without an additional process of surface stabilization or process for providing target-orientedness. Compared with conventional gold nanoparticles, the gold-protein nanoparticle fusions according to the present invention show structural stability against pH variation and concentration variation, and also have excellent target-orientedness; therefore, the fusions can bring a dramatic enhancement to the utilization of gold nanoparticles in photothermal therapy.

The invention relates to a preparation method of a biological protein-based water-tolerant wood adhesive, and belongs to the technical field of adhesive preparation. Fat and oil layer substances contained in protein-rich beancurd skin and spider silk which are taken as raw materials are used for degrading grease under the action of enzyme and microorganisms, the number of hydrophobic ester groups on the surface of protein is increased, and accordingly, the water tolerance of the protein is improved; then the protein is modified with lye, polar compact protein molecules are dispersed, and more protein subunits and hydrophobic groups in the protein are exposed, so that the contact area of the protein with wood surface is increased while the protein is water-tolerant, and the adhesion capacity of the protein is increased; then the chemical bonding force is generated between colloid and a wood substrate through the doping of wood tar, the adhesion strength of the adhesive is further improved, concentration is performed finally, and the adhesive is prepared. The prepared wood adhesive has good water tolerance, high adhesion strength and excellent application prospect.

The invention discloses a preparation method of asymmetric virus nanoparticles. The method comprises the following steps: carrying out gene modification on the virus capsid protein surface, so that the virus capsid protein simultaneously has coupled functional group and separate group; thoroughly mixing the modified virus capsid protein and wild type virus capsid protein while controlling the proportion of the two virus capsid proteins; and meanwhile, adding corresponding inorganic nanoparticles according to the total amount of the virus capsid protein to implement controllable assembly of the virus nanoparticles, thereby obtaining the asymmetric functionalized nanoparticles which are the goal product. The invention adopts biomacromolecule-protein as the nano material, and the biomacromolecule-protein can be easily modified and manually operated, and can be conveniently obtained massively. On the basis of the structural symmetry of the self-assemblable virus capsid protein, the two different protein molecules can be assembled in an oriented mode according to the previous design, and therefore, the assembly body has diversity and controllability; and the invention has the advantage of manageable reaction conditions, and can implement large-scale production.

The invention discloses a surface-enhanced Raman spectroscopy (SERS) detection method based on adsorption of proteins by hydroxyapatite nanoparticles. The SERS detection method comprises the steps of:carrying out mixed incubation on hydroxyapatite nanoparticles and a biological sample and absorbing proteins in the sample, adding acid into the mixture to adjust a pH value so as to enable the proteins to fall off from the surfaces of the hydroxyapatite nanoparticles, extracting supernate containing the fallen proteins, uniformly mixing the supernate with an SERS nano active material, detectingto obtain a biological sample protein surface enhanced Raman spectrum by utilizing an SERS technology, and establishing a biological sample protein surface enhanced Raman spectrum database; and acquiring characteristic spectral peaks of surface enhanced Raman spectra corresponding to different biological sample proteins through post-processing and analysis of the data. The SERS detection method has the advantages of quickness, simplicity in operation, low cost and the like, and can be used for effectively detecting the surface enhanced Raman spectra of the proteins in different biological samples.

Aggregation is a major cause of the misbehavior of proteins. A system for modifying a protein to create a more stable variant is provided. The method involves identifying non-conserved hydrophobic amino acid residues on the surface of a protein, suitable for mutating to more hydrophilic residues (e.g., charged amino acids). Any number of residues on the surface may be changed to create a variant that is more soluble, resistant to aggregation, has a greater ability to re-fold, and/or is more stable under a variety of conditions. The invention also provides GFP, streptavidin, and GST variants with an increased theoretical net charge created by the inventive technology. Kits are also provided for carrying out such modifications on any protein of interest.

The invention provides a fixed-point immobilization method for recombinant protein A affinity ligands. According to the method, an FGE (formylglycine generating enzyme) identification gene sequence is inserted at the tail end of a gene sequence of coding target protein with a genetic engineering means, an expression vector of the target protein is constructed, then the target protein and FGE are co-expressed in escherichia coli, and intracellular aldehyde catalytic conversion of the target protein is realized; then fixed-point immobilization is realized through selective reactions of hydrazide groups on the surface of a medium and aldehyde groups on the surface of the protein. With the adoption of the method, the target recombinant protein can be directly fixed in a broken supernatant of a cell, conditions are mild, steps are simple, the immobilization time is greatly shortened, and the immobilization cost is greatly reduced.

The invention discloses a vWF (von Willebrand factor) activity protection fluid. The vWF activity protection fluid is used in preparation for extracting von Willebrand factors from cryoprecipitated blood coagulation factor VIII waste. In a preparation technology of the von Willebrand factors, glycine is added into a chromatographic buffer solution, and lysine, glycine and albumin are added into protein fluid before freeze drying after chromatography to protect vWF activity. The vWF activity protection fluid has the advantages that by means of adding the glycine into the chromatographic buffer solution, vWF activity loss can be reduced in a chromatographic separation and purification process; the albumin, the lysine and the glycine are added into protein dialysate to serve as freeze-drying protectants, so that von Willebrand factor molecules can be stabilized; the albumin serving as an excellent protein stabilizer is capable of effectively adsorbing protein surfaces; the lysine and the glycine, serving as micromolecular amino acids, are capable of protecting a protein structure, increasing collapse temperature of a finished product and stopping protein damage caused by collapse during freeze-drying, so that biological activity is kept.

Aggregation is a major cause of the misbehavior of proteins. A system for modifying a protein to create a more stable variant is provided. The method involves identifying non-conserved hydrophobic amino acid residues on the surface of a protein, suitable for mutating to more hydrophilic residues (e.g., charged amino acids). Any number of residues on the surface may be changed to create a variant that is more soluble, resistant to aggregation, has a greater ability to re-fold, and/or is more stable under a variety of conditions. The invention also provides GFP, streptavidin, and GST variants with an increased theoretical net charge created by the inventive technology. Kits are also provided for carrying out such modifications on any protein of interest.

A computer-based method for the identification of binding targets in proteins and other macromolecules. More particularly, the invention includes an algorithm aimed at predicting binding targets in proteins. This algorithm, named Woolford, requires knowledge of the high resolution structure of the protein but no knowledge of the location or identity of natural binding sites or ligands. Binding targets in the protein are identified and classified according to their expected optimal affinities. Binding targets can be located at the protein surface or at internal surfaces that become exposed as a result of partial unfolding, conformational changes, subunit dissociation, or other events. The entire protein is mapped according to the binding potential of its constituent atoms. Once binding targets are identified, optimal ligands are designed and progressively built by the addition of individual atoms that complement structurally and energetically the selected target. This algorithm is expected to have significant applications in structure-based drug design since it allows: 1) identification of binding targets in proteins; 2) identification of additional targets if the primary target is known; 3) design of ligand molecules with optimal binding affinities for the selected target; and 4) refinement of lead compounds by defining the location and nature of chemical groups for optimal binding affinity.

The invention provides a target PPIs drug property prediction method based on a protein interaction network. The method at least comprises the following steps: S1, detecting the interaction relationship of interaction protein structural domains in the PPI network; S2, detecting a drug small molecule binding pocket on the surface of interaction protein in the PPI network; S3, obtaining a GO function similarity score of the interactive protein in the PPI network; S4, screening out PPIs meeting the following conditions at the same time to serve as drug therapy targets: protein interaction relationship pairs have structural domain interaction; in the protein interaction relationship pair, at least one protein surface has a small molecule drug binding pocket; at least two of the GO function categories of the interaction proteins of the protein interaction relationship pair have significant similarity, and the GO function categories comprise GO BP, GO MF and GO CC. According to the method, three strict mutually independent standards are adopted to comprehensively explore and discover the target PPI, false positive interaction is systematically eliminated, more reliable PPIs are selectedas drug targets, and the calculation result better conforms to objective reality.