Camelid and shark single domain antibodies: structural features and therapeutic potential

被引：142

作者：

Koenning, Doreen ^{[1
]}

Zielonka', Stefan ^{[1
]}

Grzeschik, Julius ^{[1
]}

Empting, Martin ^{[2
]}

Valldorfl, Bernhard ^{[1
]}

Krah, Simon ^{[3
]}

Schroeter, Christian ^{[3
]}

Sellmann, Carolin ^{[3
]}

Hock, Bjoern ^{[3
]}

Kolmarl, Harald ^{[1
]}

机构：

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

[2] Saarland Univ, Dept Drug Design & Optimizat, Helmholtz Inst Pharmaceut Res Saarland HIPS, Campus C2-3, D-66123 Saarbrucken, Germany

[3] Merck KGaA, Prot Engn & Antibody Technol, Frankfurter Str 250, D-64293 Darmstadt, Germany

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2017年 / 45卷

关键词：

IGNAR VARIABLE DOMAIN; THROMBOTIC THROMBOCYTOPENIC PURPURA; ANTIGEN RECEPTOR IGNAR; AFFINITY MATURATION; DISPLAY LIBRARY; CRYSTAL-STRUCTURE; PHAGE DISPLAY; LIGHT-CHAINS; IN-VIVO; SELECTION;

D O I：

10.1016/j.sbi.2016.10.019

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In addition to canonical antibodies composed of heavy and light chains, the adaptive immune systems of camelids and cartilaginous fish comprise heavy-chain only isotypes (HcAb) devoid of light chains, where antigen-binding is mediated exclusively by one variable domain. Due to their inherent favorable attributes, such as high affinity and specificity for their cognate antigen, extraordinary stability, small size and, most importantly, the possibility to complement classical antibodies in terms of 'drugable' target-space, HcAb-derived entities evolved as promising candidates for biomedical applications of which many have already proven to be successful in early stage clinical trials.

引用

页码：10 / 16

页数：7

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