7 results about "Antibody Interactions" patented technology

An arylboron compound, its preparation method, applications, and pharmaceutical compositions are disclosed for tumor imaging. The compound of formula (I) exhibits high fluorescence quantum efficiency through intramolecular charge transfer. The compound of formula (I) synthesized in this invention can be linked to different antibodies via Q3 at certain concentrations, allowing for precise targeting of corresponding tumors based on the antibody. This type of boron drug formulation can be used in boron neutron capture therapy to kill tumor cells. It exhibits better killing effects; the compound of formula (I) targets tumor cells through antigen-antibody interaction. After the boron-10-containing drug accumulates at the tumor site, neutron radiation triggers a nuclear reaction releasing alpha particles and... 7 Lithium particles kill cells; the range of these two particles is approximately 10 μm. High-energy-density heavy ions disrupt the DNA double helix structure in tumor cells, causing irreparable cell death. Simultaneously, the 10 μm distance avoids damage to normal cells and tissues.

Herein is reported a method for determining the presence of antibody-Fab-FcRn interaction in an antibody-Fc-FcRn complex influencing the in vivo half-life comprising the steps of a) determining the retention time of the antibody on an FcRn affinity chromatography column with a positive linear pH gradient elution in the presence of a first sodium chloride concentration, and b) determining the retention time of the antibody on an FcRn affinity chromatography column with a positive linear pH gradient elution in the presence of a second sodium chloride concentration, whereby the presence of antibody-Fab-FcRn interaction in an antibody-Fc-FcRn complex influencing the in vivo half-life is determined if the retention time determined in step a) and the retention time determined in step b) are substantially different.

The application patent creates a dual mode detection method, which relates to fluorescence technology and electrochemical technology. First, in a certain distance, the in-situ grown gold cluster covalent framework nanomaterial (Au@COF) can quench the fluorescence intensity of scGFP at 506 nm, and ChAT can become a bridge to shorten the distance between them and promote the quenching efficiency of the fluorescence intensity, so as to discuss the content of ChAT through the change of fluorescence intensity before and after; secondly, due to the electrostatic attraction, scGFP and GO can be well combined together, and the above material modified with ChAT antibody can be well modified to the electrode surface, when a certain amount of ChAT is added, the Au@COF modified with ChAT antibody can be further fixed to the electrode surface, and the electrode has a good electrochemical response to H2O2, and the dual mode method provides a basic theory and test method for further research on the analysis and monitoring of low concentration ChAT in cells. So far, there is no report on the choline acetyltransferase dual mode analysis method and application based on the antigen-antibody effect.

This disclosure presents an embodiment of a method for optimizing the antigen-antibody interaction potential energy matrix based on maximizing the potential energy difference. One specific implementation of this method includes: determining the average energy value of the natural complex of each training sample in a training sample set based on an initial potential energy matrix; structurally adjusting the crystal structure of the antigen-antibody complex in each training sample in the training sample set to generate a set of non-binding conformations; calculating the energy of each non-binding conformation in the set of non-binding conformations to generate a background average energy value; determining the energy difference between the average energy value of the natural complex and the background average energy value as the potential energy difference; statistically analyzing the residue pair contact frequencies of each non-binding conformation in the set of non-binding conformations to generate a residue frequency matrix; and optimizing the initial potential energy matrix to obtain an optimized potential energy matrix. This implementation can improve the accuracy of predicting antigen-antibody docking posture.

Polyacrylamide-based copolymers act as stabilizing excipients in formulations of antibody biopharmaceutical agents without interacting directly with the antibody or altering its pharmacokinetic properties. The polyacrylamide-based copolymers confer a substantial stability benefit to high concentration compositions of a variety of antibodies by precluding adsorption of the antibody to the interfaces of the composition, preventing undesirable aggregation events and maintaining the binding activity of the antibody. Such antibody compositions are useful in methods of administering the composition to a subject.

The invention is a method and computer system for determining one or more parameters quantitatively characterising the interaction between an antigen and an antibody. The method comprises producing a test region carrying an antigen that produces a first luminescence spectrum, bringing into contact with the test region a sample solution comprising an antibody that forms a complex with the antigen and produces a second luminescence spectrum different from the first luminescence spectrum, recording an image (30) or images of the test region with a digital imaging device, producing a 2D histogram (40) from intensity values of the image (30), performing curve fitting on the points of the 2D histogram (40), and determining the one or more parameters by means of the fitted curve.

The embodiment of the invention discloses an antigen-antibody interaction potential energy matrix optimization method based on potential energy difference maximization. A specific embodiment of the method comprises the steps of determining a natural compound average energy value of each training sample in a training sample set based on an initialized potential energy matrix; performing structure adjustment on the antigen-antibody complex crystal structure in each training sample in the training sample set to generate a non-binding conformation set; performing energy calculation on each non-combined conformation in the non-combined conformation set to generate a background average energy value; determining an energy difference between the natural composite average energy value and the background average energy value as a potential energy difference; performing residue pair contact frequency statistics on each non-binding conformation in the non-binding conformation set to generate a residue frequency matrix; and optimizing the initialized potential energy matrix to obtain an optimized potential energy matrix. According to the embodiment, the accuracy of antigen-antibody docking posture prediction can be improved.