8 results about "Dissociation rate" patented technology

The invention relates to the technical field of plasmas, in particular to a remote plasma source working point judgment method, device and equipment and a medium. The mass spectrum dissociation rate is calculated according to the first mass spectrum and the second mass spectrum; calculating a spectral dissociation rate according to the spectrogram; performing correction calculation on the mass spectrum dissociation rate and the spectral dissociation rate based on the initial prior Gaussian distribution model to obtain a corrected dissociation rate; when the corrected dissociation rate meets the dissociation rate required by the process, calculating an actual reaction rate according to the spectrogram and a preset emission peak height threshold value; when the actual reaction rate is equal to the reaction rate threshold value, a feedback signal reaching the process working point is generated; mass spectrum data and spectral data are mutually verified in real time, the contradiction between single-mode detection precision and process compatibility is overcome, errors such as signal attenuation, interference and peak overlapping are reduced, the reliability of dissociation rate detection is remarkably improved, meanwhile, a working point is judged in combination with correction of the dissociation rate and the actual reaction rate, stability control is enhanced, and the process precision and the yield are improved.

Disclosed herein is an anti-transferrin receptor antibody that specifically binds to the human transferrin receptor and the rhesus monkey transferrin receptor, comprising i) a humanized heavy chain variable domain derived from the heavy chain variable domain of SEQ ID NO:01, and ii) a humanized light chain variable domain derived from the light chain variable domain of SEQ ID NO:26, wherein the dissociation rate of the antibody for the human transferrin receptor is equal to or less than (i.e., at most) the dissociation rate of anti-transferrin receptor antibody 128.1 for the rhesus monkey transferrin receptor, wherein the dissociation rate is determined by surface plasmon resonance, and anti-transferrin receptor antibody 128.1 has a heavy chain variable domain of SEQ ID NO:64 and a light chain variable domain of SEQ ID NO:65.

Herein is reported an anti-transferrin receptor antibody that specifically binds to a human transferrin receptor and a macaque transferrin receptor, comprising i) a humanized heavy chain variable domain derived from the heavy chain variable domain of SEQ ID NO: 01, and ii) a humanized light chain variable domain derived from the light chain variable domain of SEQ ID NO: 26, wherein the antibody has a dissociation rate for the human transferrin receptor equal to or less than (i.e., at most) the dissociation rate of the anti-transferrin receptor antibody 128.1 for the macaque transferrin receptor wherein the dissociation rate is determined by surface plasmon resonance, and the anti-transferrin receptor antibody 128.1 has a heavy chain variable domain of SEQ ID NO: 64 and a light chain variable domain of SEQ ID NO: 65.

The present invention provides a SPARK-seq high-throughput platform for the identification and kinetics analysis of nucleic acid aptamers and target proteins thereof. By combining cell screening, CRISPR gene perturbation and single-cell multi-omics sequencing technology, the platform enables systematic identification of the interaction between thousands of nucleic acid aptamers and target proteins thereof in a single experiment; in addition, high-throughput screening of high-stability nucleic acid aptamers having "slow dissociation" characteristics is achieved on the basis of dissociation kinetics. The method provided by the present invention overcomes the limitations of the traditional technology of low throughput, difficulty in identifying targets having relatively low abundance, and inability to perform efficiently screening in natural cell environments, not only achieves large-scale and unbiased discovery of aptamer targets, but also can accurately screen high-stability aptamers having slow dissociation rates, providing more powerful molecular tools and new biomarker discovery pathways for tumor diagnosis, targeted therapy, and accurate medical treatment.

This application relates to the field of computer-aided drug design technology, and in particular to a method and system for predicting ligand-target dissociation kinetic parameters. The method includes the following steps: constructing and parameterizing a protein-ligand system; applying constraints to the system to maintain structural stability; setting multiple sets of simulation condition pairs; globally scaling the non-bonded interaction potential energy of the system or the force derived from that potential energy under each set of simulation condition pairs; performing molecular dynamics simulations and detecting ligand dissociation events under each set of simulation condition pairs; estimating the dissociation rate under each simulation condition pair; and extrapolating to the target condition based on the relationship between the dissociation rate and a unified extrapolation independent variable to obtain the dissociation rate and residence time under the target condition. This invention solves the problem in existing technologies where it is difficult to reliably obtain the dissociation rate of ligands and corresponding target receptors at an affordable computational cost, and it also features controllable parameters and ease of parallelization.

This specification provides antigen-binding protein constructs (ABPCs) that bind to TROP2 and their use. This specification provides antigen-binding protein constructs (ABPCs) and pharmaceutical compositions comprising an effective amount of ABPC, comprising a first antigen-binding domain (ABD) that can specifically bind to TROP2 or an epitope of TROP2 presented on the surface of a target mammalian cell, wherein (a) the dissociation rate of the first ABD at pH about 4.0 to about 6.5 is faster than the dissociation rate at pH about 7.0 to about 8.0, and / or (b) the dissociation constant (KD) of the first ABD at pH about 4.0 to about 6.5 is greater than the KD at pH about 7.0 to about 8.0.

Provided herein is an antigen binding protein construct (ABPC) comprising a first antigen binding domain capable of specifically binding to LRRC15 or an epitope of LRRC15 presented on the surface of a target mammalian cell, the dissociation rate of the first antigen binding domain at a pH of about 4.0 to about 6.5 is faster than the dissociation rate at a pH of about 7.0 to about 8.0; or the first antigen binding domain has a dissociation constant (KD) at a pH of about 4.0 to about 6.5 greater than a KD at a pH of about 7.0 to about 8.0.

The invention discloses a protein-ligand dissociation rate prediction method based on graph neural network transfer learning. The method belongs to the field of protein-ligand dissociation rate prediction. The method comprises the following steps: firstly, integrating a public database and literature dynamics data, and constructing a data set containing a protein structure, a ligand structure and dissociation rate parameters; pdbfixer is used for repairing a protein structure, RDkit is used for generating a ligand three-dimensional structure, and protein-ligand molecular docking is carried out through Smin. A PDBbind database is adopted to pre-train a protein-ligand affinity graph neural network model, feature coding and graph neural network processing are conducted on protein pockets and ligand molecules respectively, protein-ligand interaction information is fused through a cross attention module, and affinity prediction is achieved in combination with an energy contribution and interaction probability module. The protein-ligand dissociation rate can be efficiently and accurately predicted, and the intelligent level of drug screening and molecular design is improved.