重组DNA
表位
抗体
效应器
计算生物学
单克隆抗体
化学
蛋白质工程
生物
抗原
免疫学
生物化学
酶
基因
作者
Abhishek Singh Rathore,Animesh Sarker,Tarkeshwar Gupta
出处
期刊:Protein and Peptide Letters
[Bentham Science Publishers]
日期:2018-09-26
卷期号:25 (10): 886-896
被引量:17
标识
DOI:10.2174/0929866525666180925142757
摘要
Background: Monoclonal antibodies have been proven to deliver significant contribution in health industry for the development of both therapeutics and diagnostics. Efforts have been made to achieve immunoglobulin with high antigen specificity and stability. In this regard, smaller fragment of antibody has been constructed as an alternative of full immunoglobulin molecules due to the feasibility of recombinant production in various host cells. Antibody fragments are that part of an immunoglobulin which can form a complete epitope binding site and also retain the binding efficiency and accuracy of a whole antibody. However, the effector functions cannot be accomplished by antibody fragments alone as they lack Fc region. Hence, full antibody is constructed by fusing Fc domain of a human antibody. Nevertheless, to find an antibody with high antigen specificity and stability is still a big challenge. Conclusion: Recent protein engineering techniques have enabled many options of modification and tailoring of antibody fragments for better stability, specificity and pharmacokinetic properties. This review focuses on the latest techniques applied for the construction of antibody fragments, recent developments toward affinity maturation and applications of recombinant antibodies. Keywords: Antibody fragment, antibody engineering, therapeutic antibody, affinity maturation, single chain variable fragment, recombinant antibodies.
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