Single-domain antibodies for biomedical applications

被引：56

作者：

Krah, Simon ^{[1
]}

Schroeter, Christian ^{[1
]}

Zielonka, Stefan ^{[2
]}

Empting, Martin ^{[3
]}

Valldorf, Bernhard ^{[2
]}

Kolmar, Harald ^{[2
]}

机构：

[1] Merck KGaA, Merck Serono, Prot Engn & Antibody Technol, Darmstadt, Germany

[2] Tech Univ Darmstadt, Inst Organ Chem & Biochem, Alarich Weiss Str 4, D-64287 Darmstadt, Germany

[3] Univ Saarland, Helmholtz Inst Pharmaceut Res Saarland HIPS, Dept Drug Design & Optimizat, D-66123 Saarbrucken, Germany

来源：

IMMUNOPHARMACOLOGY AND IMMUNOTOXICOLOGY | 2016年 / 38卷 / 01期

关键词：

VHH; heavy chain antibody; Antibody engineering; antibody fragment; single chain binding domain; IgNAR; SHARK IGNAR ANTIBODY; ANTIGEN RECEPTOR IGNAR; VARIABLE DOMAINS; BIOPHYSICAL PROPERTIES; AFFINITY MATURATION; STRUCTURAL-ANALYSIS; CRYSTAL-STRUCTURE; SELECTION; FRAGMENTS; NANOBODY;

D O I：

10.3109/08923973.2015.1102934

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Single-domain antibodies are the smallest antigen-binding units of antibodies, consisting either only of one variable domain or one engineered constant domain that solely facilitates target binding. This class of antibody derivatives comprises naturally occurring variable domains derived from camelids and sharks as well as engineered human variable or constant antibody domains of the heavy or light chain. Because of their high affinity and specificity as well as stability, small size and benefit of multiple re-formatting opportunities, those molecules emerged as promising candidates for biomedical applications and some of these entities have already proven to be successful in clinical development.

引用

页码：21 / 28

页数：8

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