14 results about "Phosphorylated Peptide" patented technology

This invention relates to the field of biomedical technology, providing a phosphorylated peptide iron chelate of Yanbian cattle hemoglobin, its preparation method, and its applications. The Yanbian cattle hemoglobin phosphorylated peptide iron chelate is prepared from Yanbian cattle blood through enzymatic hydrolysis, phosphorylation, and iron chelation. Specifically, the phosphorylation step actively introduces strongly negatively charged phosphate groups into the Yanbian cattle hemoglobin peptide chain, serving as new and stronger metal ion coordination sites, thereby specifically enhancing its chelating ability for ferrous ions and the stability of the complex. The Yanbian cattle hemoglobin phosphorylated peptide iron chelate possesses high iron content and good gastrointestinal stability, showing broad application prospects in the preparation of a new generation of highly efficient and low-irritant iron supplements.

The invention relates to the field of material analytical chemistry and biochemistry, and provides a continuous batch pretreatment device and method for proteomics, glycoproteomics and phosphorylated proteomics samples. According to the continuous batch pretreatment device for the proteomics, glycoproteomics and phosphorylated proteomics samples, under the assistance of the filler, the whole process of protein denaturation, aggregation capture, enzymolysis and complete glycopeptide and phosphorylated peptide enrichment in biological samples can be achieved. Compared with a free solution method conventionally used in proteomics, the sample pretreatment method based on the device has the advantages that the sample treatment time can be effectively shortened, and continuous analysis of mass proteome, glycoprotein group and phosphorylated proteome of trace protein samples can be realized; the method is expected to be widely applied to the aspects of disease occurrence mechanisms, drug action mechanisms, clinical detection, biomarker discovery and the like.

The application discloses an amino-functionalized magnetic mesoporous nanomaterial and a preparation method and application thereof, and the nanomaterial is Fe3O4@nSiO2@TiO2@mSiO2-NH2; from inside to outside, the nanomaterial comprises a magnetite magnetic core, a dense silica layer, a titanium dioxide layer and an amino-functionalized mesoporous silica layer. The magnetic core is synthesized by a solvothermal method, the dense silica layer and the titanium dioxide layer are coated by adopting a sol-gel method in sequence, and finally the amino-functionalized mesoporous silica layer is modified by a co-condensation method. The material can protonate the surface amino group to form a local alkaline microenvironment under an acidic condition, can maintain trypsin activity, realizes synchronous performance of rapid enzymolysis of proteins and in-situ enrichment of phosphorylated peptides, and significantly shortens the enzymolysis time. The application has excellent enrichment selectivity for the phosphorylated peptides, the sensitivity reaches 10 fmol / μL, the enrichment capacity is about 100 mg / g, and is suitable for high-throughput quantitative analysis of phosphorylated proteins in complex biological samples.

This invention relates to a TiO2 / Ti3C2T based on multiple crystal forms. x This invention relates to composite materials, their preparation methods, and their application in the selective enrichment of phosphorylated peptides, encompassing the fields of novel biomaterials and phosphorylated peptide enrichment technology. The invention pertains to TiO2 / Ti3C2T. x The preparation methods of composite materials include: (1) Ti3C2T x Preparation of layered materials, (2) TiO2 / Ti3C2T with multiple crystal forms x The preparation of composite materials yielded anatase, rutile, and mixed anatase and rutile TiO2 / Ti3C2T composites. x Composite materials, and different crystal forms of TiO2 / Ti3C2T x The composite material is used for the enrichment of phosphorylated peptides, while simultaneously regulating the TiO2 / Ti3C2T ratio. x The crystal form of TiO2 in composite materials can also effectively regulate the material's ability to enrich phosphorylated peptides, thereby greatly improving the enrichment efficiency of phosphorylated peptides.

A method for early diagnosis or stage classification of Alzheimer's disease includes obtaining a tau protein-derived phosphorylated peptide from an isolated biological sample and quantifying the tau protein-derived phosphorylated peptide. Through the quantification of tau protein-derived phosphorylated peptides, it is possible to effectively diagnose Alzheimer's disease at an early stage or classify its stages, and determine the accumulation of amyloid beta in the brain.

The invention discloses hydrogel containing 7-amino acid phosphorylated peptide and application of the hydrogel in neural restoration. The hydrogel comprises acellular matrix hydrogel, 7-amino acid phosphorylated peptide, 7-amino acid phosphorylated peptide, 7-amino acid phosphorylated peptide and 7-amino acid phosphorylated peptide, and a 7-amino acid phosphorylated peptide supported in the acellular matrix hydrogel. The 2, 7-amino acid phosphorylated peptide can play a multi-dimensional regulation role in nerve injury microenvironment remodeling, realizes dynamic targeted regulation of peripheral nerve injury microenvironment, and promotes rapid regeneration and recovery of injured peripheral nerves.

This invention discloses a single-sample multi-omics component extraction method for multi-omics joint analysis. The method includes: adding nucleic acid extraction solution to the sample, transferring it to a DNA adsorption column, centrifuging, and collecting the filtrate; washing the DNA adsorption column; eluting DNA; adding ethanol to the filtrate, transferring it to an RNA adsorption column, centrifuging, and collecting the filtrate; washing the RNA adsorption column; eluting RNA; and extracting proteins. This method integrates centrifugation column-based DNA / RNA co-extraction technology, a zinc ion-mediated protein precipitation and capture strategy, and an efficient Fe-IMAC phosphorylated peptide enrichment process. It achieves efficient protein precipitation and in-situ washing, thoroughly removing chemical components that interfere with mass spectrometry detection. It simultaneously achieves high-quality nucleic acid extraction and deep proteomics and phosphorylated proteomics coverage in a single sample, effectively solving the bottlenecks of traditional methods such as limited sample size, complex procedures, and poor reproducibility.

This invention relates to a cell-penetrating peptide Y119E and its application in inhibiting the growth of cisplatin-resistant tumors. The invention is characterized by using the cell-penetrating peptide TAT as a carrier to deliver a cell-penetrating peptide containing PGAM1 phosphorylated at position Y119 into tumor cells. The cell-penetrating peptide containing Y119 phosphorylated peptide (Y119E) has the sequence YGRKKRRQRRR-KIWRRSEDVP. The short cell-penetrating peptide Y119E is used in the drug application of inhibiting the growth of cisplatin-resistant tumors. It can effectively inhibit tumor growth subcutaneously in nude mice.

The invention relates to the field of protein detection, in particular to a phosphorylated peptide fragment preparation and space phosphorylated proteomics detection method. By means of the preparation method, enough phosphorylated peptide fragments can be efficiently extracted from a trace sample, the method can be compatible with LCM for use, operation is easy and convenient, the recovery rate is high, and the method is suitable for achieving high-depth space phosphorylated proteomics analysis. Meanwhile, the analysis method shows high sensitivity on the trace level, and compared with a traditional method, the identification number of phosphorylation sites is remarkably increased. Compared with the homogenization treatment of the whole section, the analysis method provided by the invention can more accurately reflect the specificity of the cells in the target area and better reflect the intra-tumor heterogeneity.

The invention belongs to the technical field of proteomics, and particularly relates to a phosphorylated peptide fragment enrichment identification method for trace tissues. The method comprises the following steps: (1) adding a lysis solution into a trace tissue sample, and heating; performing ultrasonic treatment on the sample in an ice-water bath; adding enzyme for enzymolysis; adding a solution containing a phosphopeptide enrichment material into the sample for incubation; activating and balancing a peptide fragment desalting column by using two enrichment buffer solutions; (2) adding a sample and a mixed solution containing the phosphopeptide enrichment material into the pretreated desalting column; cleaning with a cleaning buffer solution A and a cleaning buffer solution in sequence; eluting with two elution buffer solutions in sequence; and collecting the eluent, and carrying out vacuum concentration and freeze-drying to obtain the enriched phosphorylated peptide fragment of the trace tissue sample. The method can reduce treatment steps and reduce liquid transfer, so that sample loss can be reduced; the pretreatment time is greatly saved; the identification of the phosphorylation site of the protein with the initial quantity as low as 10 ng is realized.

The application discloses a kind of mesoporous silica as base, natural biomolecule chondroitin sulfate as modified phase functional composite material.The preparation method of the material is disclosed simultaneously, with Glymo silane reagent as connecting arm, polyethylene imine is grafted to the surface of mesoporous silica, then by polyethylene imine and chondroitin sulfate Michael addition reaction obtains chondroitin sulfate modified mesoporous silica material (MSN-PEI-CS).Material is determined by TEM, and with human serum immunoglobulin G as model sample, the selective enrichment effect of material to glycopeptide is explored.The experimental results show that the material shows good detection limit, enrichment capacity and enrichment selectivity.The material is post-modified to introduce Ti 4+ MSN-PEI-CS-PO3 2‑ -Ti 4+ , glycopeptide and phosphorylated peptide can be co-enriched.The MSN-PEI-CS and derived material MSN-PEI-CS-PO3 2‑ -Ti 4+ of the application have wide application prospect in post-translational modification proteomics, and provide new ideas for material design.

Liposomes or conjugates of tau peptides and methods for their use to prevent or treat tauopathies, such as Alzheimer's disease, are provided. The present invention provides a liposome containing a tau peptide, preferably a phosphorylated tau peptide, and a conjugate containing a tau peptide, preferably a phosphorylated tau peptide, conjugated to an immunogenic carrier.

The application discloses a preparation of immobilized bimetallic ion affinity chromatography porous material and a method for ultrafast enrichment of N-phosphorylated peptides under acidic conditions, and relates to the technical field of analytical chemistry. The method comprises uniformly dispersing phosphorylated degreasing cotton and titanium salt and zirconium salt in a trifluoroacetic acid aqueous solution, and reacting at room temperature to obtain the immobilized bimetallic ion affinity chromatography porous material. The Ti@Zr-PC porous material prepared by the application has an optimal enrichment effect on N-phosphorylated peptide segments in biological samples, and the Ti@Zr-PC material has high permeability and high metal ion modification density. N ​

This invention discloses a polyurea-functionalized macroporous adsorption resin microsphere material and its applications. Specifically, macroporous adsorption resin microspheres are used as the matrix, and terephthalic diisocyanate and tri-(2-aminoethyl)amine are used as functional monomers. Through isocyanate-amine polymerization and epoxy-amine ring-opening reaction, a polyurea-rich crosslinked network is bonded and coated onto the surface of the resin microspheres, resulting in surface polyurea-functionalized macroporous adsorption resin (MAR@PUP) microspheres. The surface of MAR@PUP microspheres is rich in urea groups, which can recognize phosphorylation sites in peptides through multiple hydrogen bonds. Based on the differences in phosphorylation degree and the regulation of enrichment conditions, highly selective enrichment of monophosphorylated peptides and polyphosphorylated peptides can be achieved, especially showing excellent enrichment performance for polyphosphorylated peptides.