[Single-domain antibody - advances in research and application]

Area of Science:

• Biochemistry
• Immunology
• Molecular Biology

Background:

• Conventional IgG antibodies consist of heavy and light chains with distinct variable and constant regions.
• Single domain antibodies (sdAbs), or nanobodies, are derived from the variable domain of the heavy chain, lacking light chains.
• Despite their simpler structure, sdAbs demonstrate comparable or enhanced antigen-binding affinity compared to conventional antibodies.

Purpose of the Study:

• To review the structural characteristics of single domain antibodies (sdAbs).
• To discuss the physicochemical properties and screening strategies for sdAbs.
• To highlight recent advancements in the application of sdAbs in biomedical research and clinical settings.

Main Methods:

• Literature review of structural features, physicochemical properties, and screening strategies for sdAbs.
• Analysis of recent research on the applications of sdAbs in fundamental biomedical research.
• Synthesis of information on clinical applications and advancements in sdAb technology.

Main Results:

• sdAbs possess a unique structure comprising only a variable heavy chain domain.
• Key advantages of sdAbs include their small size, high stability, and straightforward recombinant expression.
• sdAbs exhibit significant potential in various biomedical research and clinical applications.

Conclusions:

• Single domain antibodies represent a promising class of therapeutic and diagnostic agents.
• The unique properties of sdAbs facilitate their use in diverse scientific and medical fields.
• Further research into sdAb development and application is warranted to fully exploit their potential.