Literature DB >> 31915934

Assessment of Antibody Self-Interaction by Bio-Layer-Interferometry as a Tool for Early Stage Formulation Development.

Martin Domnowski1,2, Jan Jaehrling2, Wolfgang Frieß3.   

Abstract

PURPOSE: To speed up the drug development process in the biopharmaceutical industry, high throughput methods are indispensable for assessing drug candidates and potential lead formulations, in particular during late stages of discovery and early phases of development. This study aimed to establish a bio-layer-interferometry based high throughput assay for assessing formulation dependent mAb self-interaction (SI-BLI) and to compare the results with kD values obtained by dynamic light scattering (DLS).
METHODS: Self-interaction of proprietary and commercially available mAbs was analyzed by SI-BLI and dynamic light scattering (DLS).
RESULTS: We found significant correlations of the SI-BLI results and kD-values obtained by DLS for both, different mAbs in one platform formulation and for mAbs formulated in several buffer compositions. In total, we assessed self-interaction propensity of different mAbs in 58 formulations and found significant Pearson correlation (p < 0.05) between kD and results of SI-BLI.
CONCLUSIONS: The SI-BLI results correlate with kD and enable fast ranking of both different drug candidates and potential lead formulations. Thus, SI-BLI might decrease the risk to lose potent mAb candidates during transition from discovery to development, and help to accelerate the development of high concentration liquid formulations.

Keywords:  Self-interaction; antibody; bio-layer-interferometry; diffusion interaction parameter; high concentration formulation

Mesh:

Substances:

Year:  2020        PMID: 31915934     DOI: 10.1007/s11095-019-2722-4

Source DB:  PubMed          Journal:  Pharm Res        ISSN: 0724-8741            Impact factor:   4.200


  29 in total

Review 1.  Molecular basis of high viscosity in concentrated antibody solutions: Strategies for high concentration drug product development.

Authors:  Dheeraj S Tomar; Sandeep Kumar; Satish K Singh; Sumit Goswami; Li Li
Journal:  MAbs       Date:  2016-01-06       Impact factor: 5.857

2.  Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution.

Authors:  Jun Liu; Mary D H Nguyen; James D Andya; Steven J Shire
Journal:  J Pharm Sci       Date:  2005-09       Impact factor: 3.534

3.  Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity.

Authors:  Sonoko Kanai; Jun Liu; Thomas W Patapoff; Steven J Shire
Journal:  J Pharm Sci       Date:  2008-10       Impact factor: 3.534

4.  Specific interactions in high concentration antibody solutions resulting in high viscosity.

Authors:  Sandeep Yadav; Jun Liu; Steven J Shire; Devendra S Kalonia
Journal:  J Pharm Sci       Date:  2010-03       Impact factor: 3.534

5.  Monoclonal antibody self-association, cluster formation, and rheology at high concentrations.

Authors:  Wayne G Lilyestrom; Sandeep Yadav; Steven J Shire; Thomas M Scherer
Journal:  J Phys Chem B       Date:  2013-05-17       Impact factor: 2.991

6.  Concentration dependent viscosity of monoclonal antibody solutions: explaining experimental behavior in terms of molecular properties.

Authors:  Li Li; Sandeep Kumar; Patrick M Buck; Christopher Burns; Janelle Lavoie; Satish K Singh; Nicholas W Warne; Pilarin Nichols; Nicholas Luksha; Davin Boardman
Journal:  Pharm Res       Date:  2014-06-07       Impact factor: 4.200

7.  Measurements of Monoclonal Antibody Self-Association Are Correlated with Complex Biophysical Properties.

Authors:  Steven B Geng; Michael Wittekind; Adam Vigil; Peter M Tessier
Journal:  Mol Pharm       Date:  2016-04-19       Impact factor: 4.939

8.  Prediction of Protein Aggregation in High Concentration Protein Solutions Utilizing Protein-Protein Interactions Determined by Low Volume Static Light Scattering.

Authors:  Melanie Hofmann; Matthias Winzer; Christian Weber; Henning Gieseler
Journal:  J Pharm Sci       Date:  2016-05-06       Impact factor: 3.534

9.  Charge-mediated Fab-Fc interactions in an IgG1 antibody induce reversible self-association, cluster formation, and elevated viscosity.

Authors:  Jayant Arora; Yue Hu; Reza Esfandiary; Hasige A Sathish; Steven M Bishop; Sangeeta B Joshi; C Russell Middaugh; David B Volkin; David D Weis
Journal:  MAbs       Date:  2016-08-25       Impact factor: 5.857

10.  Self-Interaction Chromatography of mAbs: Accurate Measurement of Dead Volumes.

Authors:  S H M Hedberg; J Y Y Heng; D R Williams; J M Liddell
Journal:  Pharm Res       Date:  2015-08-13       Impact factor: 4.200

View more
  1 in total

1.  Binding behavior of spike protein and receptor binding domain of the SARS-CoV-2 virus at different environmental conditions.

Authors:  Meiyi Zhang; Haoqi Wang; Emma R Foster; Zivko L Nikolov; Sandun D Fernando; Maria D King
Journal:  Sci Rep       Date:  2022-01-17       Impact factor: 4.379

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.