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A New Approach to Assess mAb Aggregation.

Illarion V Turko1,2

  • 1Biomolecular Mesurement Division, National Institute of Standards and Technology, Gaithersburg, MD, USA. illarion.turko@nist.gov.

Methods in Molecular Biology (Clifton, N.J.)
|March 13, 2020
PubMed
Summary

A new method uses phage display peptides to detect and quantify monoclonal antibody (mAb) aggregation. This peptide-binding assay with fluorescence polarization offers a way to monitor therapeutic protein aggregation propensity.

Keywords:
AggregationFITC-peptideMonoclonal antibodiesNext-generation sequencingPeptide phage display

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Area of Science:

  • Biochemistry
  • Biotechnology
  • Pharmaceutical Science

Background:

  • Monoclonal antibodies (mAbs) are crucial biotherapeutics.
  • MAb aggregation is a significant concern affecting drug safety and efficacy.
  • Current methods for detecting mAb aggregation can be complex or lack sensitivity.

Purpose of the Study:

  • To develop a novel methodology for detecting and quantifying mAb aggregation.
  • To identify specific peptides that recognize aggregated mAbs.
  • To establish a sensitive assay for monitoring protein aggregation.

Main Methods:

  • Screening of a phage display peptide library using aggregated mAbs as bait.
  • Selection of peptides with affinity for mAb aggregates.
  • Development of a homogeneous assay using peptide-binding and fluorescence polarization detection.

Main Results:

  • Successfully identified peptides capable of recognizing mAb aggregates.
  • Demonstrated the ability of the peptide-binding method coupled with fluorescence polarization to detect mAb aggregation.
  • Indicated potential for quantitative assessment of mAb aggregation.

Conclusions:

  • A proof-of-concept for a new mAb aggregation detection methodology was established.
  • Selected peptides can serve as recognition elements in novel diagnostic assays.
  • The developed assay shows promise for monitoring the aggregation propensity of therapeutic proteins.