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Conformational stability and aggregation of therapeutic monoclonal antibodies studied with ANS and Thioflavin T binding.

ABSTRACT: Characterization of aggregation profiles of monoclonal antibodies (mAb) is gaining importance because an increasing number of mAb-based therapeutics are entering clinical studies and gaining marketing approval. To develop a successful formulation, it is imperative to identify the critical biochemical properties of each potential mAb drug candidate. We investigated the conformational change and aggregation of a human IgG1 using external dye-binding experiments with fluorescence spectroscopy and compared the aggregation profiles obtained to the results of size-exclusion chromatography. We show that using an appropriate dye at selected mAb concentration, unfolding or aggregation can be studied. In addition, dye-binding experiments may be used as conventional assays to study therapeutic mAb stability.

SUBMITTER: Kayser V

PROVIDER: S-EPMC3218538 | biostudies-literature | 2011 Jul-Aug

REPOSITORIES: biostudies-literature

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Conformational stability and aggregation of therapeutic monoclonal antibodies studied with ANS and Thioflavin T binding.

Kayser Veysel V Chennamsetty Naresh N Voynov Vladimir V Helk Bernhard B Trout Bernhardt L BL

mAbs 20110701 4

Characterization of aggregation profiles of monoclonal antibodies (mAb) is gaining importance because an increasing number of mAb-based therapeutics are entering clinical studies and gaining marketing approval. To develop a successful formulation, it is imperative to identify the critical biochemical properties of each potential mAb drug candidate. We investigated the conformational change and aggregation of a human IgG1 using external dye-binding experiments with fluorescence spectroscopy and c ...[more]

PMID: 21540645

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