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Recent Developments Toward Antibody Engineering and Affinity Maturation.

Authors
  • Rathore, Abhishek S1
  • Sarker, Animesh1
  • Gupta, Rinkoo D1
  • 1 Faculty of Life Sciences and Biotechnology, South Asian University, New Delhi-110021, India. , (India)
Type
Published Article
Journal
Protein and peptide letters
Publication Date
Jan 01, 2018
Volume
25
Issue
10
Pages
886–896
Identifiers
DOI: 10.2174/0929866525666180925142757
PMID: 30255742
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

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. 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. Copyright© Bentham Science Publishers; For any queries, please email at [email protected]

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