相关实验视频

Updated: Jul 10, 2025

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Determination of High-affinity Antibody-antigen Binding Kinetics Using Four Biosensor Platforms

Published on: April 17, 2017

对数据驱动抗体设计的相互作用动力学的高通量分析系统

Ryo Matsunaga^1,2, Kan Ujiie¹, Mayuko Inagaki¹

¹Department of Bioengineering, School of Engineering, The University of Tokyo, Tokyo, 113-8656, Japan.

Scientific reports

|November 22, 2023

概括

我们开发了BreviA,这是一种高通量表面等离子体共振 (SPR) 系统,用于抗体查. 这种系统加速了抗体动力学分析,使得能够快速发现高亲和力的抗体,例如那些准编程细胞死亡蛋白1 (PD-1) 的抗体.

科学领域:

生物技术是生物技术.
免疫学免疫学免疫学
分子生物学分子生物学

背景情况:

表面等离子体共振 (SPR) 是分析抗原-抗体相互作用的宝贵工具.
目前的SPR应用在选阶段受到限制,因为吞吐量低.
需要高通量方法来加速抗体的发现和表征.

研究的目的:

开发一种名为BreviA.A.的新型高通量SPR分析系统.
为了使抗体库的快速选和动力学分析.
为了证明系统在抗体工程和优化中的实用性.

主要方法:

利用Brevibacillus表达系统进行抗体生产.
构建了一个可编码多种抗体序列的等离子体库.
基于细菌细胞的综合序列分析与SPR.的超级抗体固定化.
对针对抗原的抗体突变体进行了高通量SPR选.

主要成果:

布雷维亚系统促进了高通量选,在一周内可进行多达384次相互作用分析.
在设计一种抗编程细胞死亡蛋白1 (PD-1) 抗体以增强小鼠PD-1亲和力的过程中成功应用.
通过深度突变扫描识别了显著增加抗体亲和力 (>100倍) 的特定突变.

结论:

布雷维亚系统显著提高了基于SPR的抗体查的吞吐量.
这个平台加速了数据驱动的抗体设计和优化.
布雷维亚显示出抗体快速发展的潜力,具有更好的特异性和亲和力.

更多相关视频

Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries

Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries

Published on: January 17, 2015

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

相关概念视频

Protein Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...