antibody aggregation: insights from sequence and structure

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ID: 173206
2016
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Abstract
Monoclonal antibodies (mAbs) are the fastest-growing biological therapeutics with important applications ranging from cancers, autoimmunity diseases and metabolic disorders to emerging infectious diseases. Aggregation of mAbs continues to be a major problem in their developability. Antibody aggregation could be triggered by partial unfolding of its domains, leading to monomer-monomer association followed by nucleation and growth. Although the aggregation propensities of antibodies and antibody-based proteins can be affected by the external experimental conditions, they are strongly dependent on the intrinsic antibody properties as determined by their sequences and structures. In this review, we describe how the unfolding and aggregation susceptibilities of IgG could be related to their cognate sequences and structures. The impact of antibody domain structures on thermostability and aggregation propensities, and effective strategies to reduce aggregation are discussed. Finally, the aggregation of antibody-drug conjugates (ADCs) as related to their sequence/structure, linker payload, conjugation chemistry and drug-antibody ratio (DAR) is reviewed.
Reference Key
li2016antibodiesantibody Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Wei Li;Ponraj Prabakaran;Weizao Chen;Zhongyu Zhu;Yang Feng;Dimiter S. Dimitrov
Journal analytical methods
Year 2016
DOI
10.3390/antib5030019
URL
http://www.mdpi.com/2073-4468/5/3/19
Keywords
monoclonal antibodies protein unfolding allergy

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