相关实验视频
Updated: Jun 24, 2025

09:05
Determining the Phagocytic Activity of Clinical Antibody Samples
Published on: November 30, 2011
23.5K
洞察IgG和FcRn之间的双价值,pH依赖的相互作用的热情-亲和关系
Johannes Reusch1,2, Jan Terje Andersen3,4,5, Ulrich Rant1
1Dynamic Biosensors GmbH, Munich, Germany.
mAbs
|June 7, 2024
概括
这项研究引入了switchSENSE技术,用于分析单克隆抗体与新生儿Fc受体 (FcRn) 通过pH梯度的复杂结合. 这些发现揭示了对抗体-FcRn相互作用的关键见解,指导了未来的治疗工程.
科学领域:
- 生物化学 生化学
- 免疫学 免疫学 免疫学
- 药理学 药理学 是一个学科.
背景情况:
- 单克隆抗体 (mAbs) 需要有利的药理动力学,如延长血清半衰期,以获得治疗疗效.
- 这个半衰期是由与新生儿Fc受体 (FcRn) 的pH依赖性结合调节的.
- 之前的研究集中在单一亲和值上,忽视了IgG在内体pH梯度上的双重FcRn结合潜力.
研究的目的:
- 综合分析IgG-FcRn相互作用,强调亲和和热情.
- 为了研究生理学pH范围内的热情与亲和关系.
- 评估switchSENSE技术对于FcRn结合动力学分析的实用性.
主要方法:
- 使用了switchSENSE技术,在DNA纳米上固定了复合FcRn.
- 通过pH梯度 (pH 5.87.4) 评估结合动力学.
- 将switchSENSE的性能与经典的表面等离子共振 (SPR) 和其他方法进行比较.
主要成果:
- 鉴定了工程IgG1-YTE的pH7.2的亲和性拐点,表明增强的FcRn结合.
- 观察到IgG1-YTE的pH开关在pH 6.2时增强欲,而pH 7.4.4时欲被废除.
- 与SPR.相比,证明了switchSENSE在区分亲和力和狂热的卓越能力.
结论:
- switchSENSE为IgG-FcRn结合模式及其pH依赖关系提供可靠的动力学参数.
- 该方法可以解读变量Fab臂对FcRn结合的影响,这是SPR的限制.
- 这项研究为设计具有优化FcRn结合性质的IgG分子提供了指导,以改善治疗策略.
更多相关视频
相关概念视频
Affinity and Avidity
36.0K
Overview
36.0K
Diversity of Antigen Receptors
568
Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
568
Immunoglobulin-like Cell Adhesion Molecules
3.2K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
3.2K
Antibody Structure
60.0K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
60.0K
Antibody Structure and Classes
877
Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
877
Antibody Actions
1.1K
Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
1.1K

