11 results about "Competitive binding" patented technology

A computer-implemented framework for designing high-efficiency and high-specificity nucleic acid molecules targeting transfer RNA (tRNA) and its derivatives (tDRs). The framework comprises two primary algorithms. The first, tBOND-G, designs guide RNAs (gRNAs) for Cas13-mediated tRNA cleavage by calculating physical parameters, including target site accessibility and binding energy, and processing them through a Support Vector Machine (SVM) model to predict cleavage efficiency. The second algorithm, tBOND-L, designs therapeutic Locked Nucleic Acid-modified antisense oligonucleotides (LNA-ASOs) that specifically target a tDR without binding to its parent tRNA. This method utilizes a processor to derive an efficiency score based on relative binding affinity and a specificity score based on simulated competitive binding environments.

This invention belongs to the field of biomedicine and discloses the application of palmitoyltransferase ZDHHC21 in the preparation of drugs for treating breast cancer. This invention demonstrates that ZDHHC21 knockdown upregulates RIPK1 expression, which is related to signal feedback induced by CD82 palmitoylation deficiency. Depalmitoylated CD82 competitively binds to RIPK1 inhibitory molecules, thereby releasing the regulation of RIPK1, promoting the interaction and phosphorylation activation of RIPK1 and RIPK3, and subsequently upregulating MLKL expression and inducing its activation. Downstream activation of Caspase-3 ultimately initiates necroptosis. A specific regulatory axis of "ZDHHC21–CD82–pan-apoptosis" is established. This provides a potential novel therapeutic target for triple-negative breast cancer and offers a theoretical and experimental basis for therapeutic strategies targeting tumor cell death. Further research can explore the role of this regulatory axis in vivo, providing support for clinical translation.

This invention discloses a highly sensitive LCN2 detection kit and its preparation method for assessing the prognostic risk of patients with stress-induced cardiomyopathy. The kit contains a signal probe composed of rare-earth-doped upconversion nanoparticles and an LCN2-specific DNA aptamer, as well as a complementary oligonucleotide quenching probe with a quenching group. Its core principle is based on fluorescence resonance energy transfer regulated by competitive binding: when the target protein LCN2 is absent, the binding of the two probes leads to luminescence quenching; when LCN2 is present, they competitively bind to the aptamer and dissociate the quenching probe, thereby restoring upconversion luminescence. This homogeneous detection method effectively avoids the interference of autofluorescence in biological samples by utilizing near-infrared excitation. Combined with the high stability and specificity of the aptamer, it achieves a simple, rapid, highly specific, and ultra-sensitive quantitative detection of LCN2 protein in serum, providing a reliable tool for clinical prognostic assessment.

This invention discloses the use of oligomycin A in the preparation of a drug for competitively inhibiting EphB3 to reverse lorlatinib resistance, belonging to the field of biomedical technology. This invention experimentally discovered that EphB3 is a key factor mediating lorlatinib resistance in lung cancer, and that existing oligomycin A can effectively reverse EphB3-mediated resistance by competitively binding to EphB3. Based on this, this invention protects the use of oligomycin A in the preparation of a drug for reversing lorlatinib resistance in tumors (especially ALK-positive non-small cell lung cancer). Simultaneously, this invention also protects a therapeutically effective pharmaceutical composition comprising oligomycin A and lorlatinib, and a non-therapeutic method for reversing cellular resistance to lorlatinib in vitro. This invention provides a novel and effective solution for overcoming lorlatinib resistance in clinical practice.

A specific polypeptide interfering with the binding of Rac1 and PAK2, a pharmaceutical composition thereof and application, the amino acid sequence of the specific polypeptide is shown as SEQ ID NO:1; the polypeptide blocks the binding of Rac1 and the 81-85 amino acids (EHTIH) of PAK2 protein by competitive binding, inhibits the phosphorylation of PAK2 and the activation of downstream TGF-beta, alpha-SMA and collagen I fibrosis pathway. The application discloses a pharmaceutical composition comprising the polypeptide and application of the polypeptide in preparation of a medicine for treating diabetic kidney fibrosis. In vitro cell experiments show that the polypeptide inhibits the increase of p-PAK2 and the expression of fibrosis factors induced by high glucose in vitro; animal experiments show that the polypeptide can improve the pathological damage of the kidney of diabetic mice, reduce the expression of fibrosis-related factors, and has high specificity and long-acting property, thereby providing a new direction and method for the treatment of diabetic kidney fibrosis.

This invention discloses a two-dimensional liquid chromatography (HPLC) method for determining lactoferrin in infant formula. Based on online purification HPLC technology, the first dimension uses a heparin affinity column, and the second dimension uses a reversed-phase C4 column. This method achieves accurate qualitative and quantitative analysis of lactoferrin in infant formula. By adding Tween-20 and sodium chloride to the extract, non-specific adsorption and competitive binding in complex matrices are effectively inhibited, significantly improving the recovery rate of lactoferrin (93.5%–97.3%). The method exhibits good linearity in the range of 5–200 μg / mL, with a detection limit of 2 mg / 100g, a quantitation limit of 5 mg / 100g, and an RSD of 1.2%–3.9%, providing accurate and reliable results. Optimized flow path and cleaning procedures enable online two-dimensional purification and analysis, allowing the expensive heparin affinity column to be reused and reducing detection costs.

A method is provided for determining the potency of a human neonatal Fc receptor (FcRn) antagonist composition in inhibiting the binding of human IgG to FcRn using a competitive binding assay. A kit for performing said method is also provided, as well as a method for manufacturing the FcRn antagonist composition, including the method for determining potency.

This invention discloses a dissociation agent, its preparation method, and its applications. The dissociation agent comprises a chelating agent, a competitive binding agent, an inclusion agent, a denaturing agent, a surfactant system, a stabilizer, and a buffer system. The competitive binding agent is salicylic acid, the inclusion agent is hydroxypropyl-β-cyclodextrin, and the surfactant system is a compound system of the nonionic surfactant Brij-35 and the amphoteric surfactant 3-sulfopropyltetradecyl dimethyl betaine. This invention efficiently dissociates bound hormones through multiple synergistic effects of chelation, competition, inclusion, and denaturation; the components are mild, have good compatibility with chemiluminescence detection systems, and do not interfere with the detection signal; simultaneously, the addition of stabilizers and preservatives significantly improves the long-term stability of the reagent. This invention exhibits high dissociation efficiency, strong stability, and simple operation, with a correlation of over 0.99 with imported reagents, demonstrating promising clinical application prospects and industrialization value.

This invention discloses an ELISA method and its application based on liposome nanovesicles, belonging to the field of biotechnology. The invention prepares HRP-coated and biotinylated liposome nanovesicles using phospholipids, sterol derivatives, and biotinylated polyethylene glycol phospholipids as raw materials. These nanovesicles are highly sensitive to acidic environments of pH 3-6, specifically recognizing streptavidin. Under acidic conditions, they cleave to release HRP and catalyze substrate color development. Using these nanovesicles as tracers, an ELISA is established based on the principle of antigen-antibody competitive binding to achieve the detection of thiamethoxam residues, a neonicotinoid insecticide. The method of this invention has a detection limit as low as 0.24 µg / L for thiamethoxam, exhibiting high sensitivity, simple operation, economy, speed, and high-throughput screening capabilities. It is suitable for the detection of thiamethoxam residues in agricultural products, soil, and water bodies, solving the technical problem of low sensitivity in traditional ELISA methods.

This invention proposes a capsaicin nucleic acid aptamer and its ratiometric fluorescent biosensor application. A capsaicin-specific nucleic acid aptamer with nanomolar affinity for capsaicin was obtained using the RNase-SELEX screening strategy. Furthermore, a ratiometric fluorescent biosensor was constructed using the pruned aptamer. A dual-signal response is achieved through competitive binding / conformational regulation of the aptamer by capsaicin and the nucleic acid dye SYBR Green II. Quantitative detection of capsaicin is achieved through a linear relationship between the fluorescence ratio and capsaicin concentration, exhibiting advantages such as high sensitivity and strong anti-interference capability.

Provided are a group of PD-1 molecules and mutants thereof that block the binding of anti-PD-1 antibodies to cell surface PD-1 molecules and uses thereof. Also provided is a protein molecule that has 80%-100% sequence identity compared to a wild-type protein shown in SEQ ID NO: 1. The provided recombinant protein H126 and H134 molecules can competitively bind to an anti-PD-1 antibody drug expressed by T cell endogenous PD-1 molecules without affecting the binding of PD-1 to endogenous PD-L1 molecules, thereby restoring the functional inhibition of activated T cells and alleviating the symptoms of immune therapy-related adverse reactions. The protein molecules provide a new approach for the clinical treatment of immune therapy-related adverse reactions.