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Global kinetic analysis of seeded BSA aggregation.

Ziya Sahin1, Yusuf Kemal Demir1, Veysel Kayser1

  • 1Faculty of Pharmacy, The University of Sydney, Sydney, NSW, Australia.

European Journal of Pharmaceutical Sciences : Official Journal of the European Federation for Pharmaceutical Sciences
|March 13, 2016
PubMed
Summary

Seeded bovine serum albumin (BSA) aggregation kinetics near its melting temperature (Tm) reveal two main pathways: monomer addition and aggregate-aggregate interactions. Aggregate-aggregate interactions dominate, especially with pre-existing seeds, impacting biopharmaceutical stability.

Keywords:
Accelerated studiesAggregation mechanismsArrhenius kineticsGlobal analysisKinetic modellingSeeded protein aggregation

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Pharmaceutical Sciences

Background:

  • Understanding protein aggregation is crucial for biopharmaceutical stability and shelf-life.
  • Bovine serum albumin (BSA) is a model protein frequently used in aggregation studies.
  • Seeding can significantly influence protein aggregation pathways and kinetics.

Purpose of the Study:

  • To investigate the kinetics and mechanisms of seeded BSA aggregation around its melting temperature (Tm).
  • To differentiate between monomer addition and aggregate-aggregate interaction pathways.
  • To explore the implications of aggregation mechanisms on biopharmaceutical shelf-life and data interpretation.

Main Methods:

  • Accelerated aggregation studies conducted near the melting temperature (Tm) of BSA.
  • Tracking aggregation using Size Exclusion Chromatography High-Performance Liquid Chromatography (SEC-HPLC).
  • Monitoring aggregation via intrinsic fluorescence spectroscopy.
  • Global kinetic analysis of monomer, dimer, and soluble aggregate concentrations.

Main Results:

  • BSA aggregation is irreversible and proceeds via sequential monomer addition and aggregate-aggregate interactions.
  • Sequential monomer addition occurs only with non-native monomers, initiating 1-2°C below Tm.
  • Aggregate-aggregate interactions are the dominant mechanism below Tm, driven by seeding aggregates.
  • Aggregate-aggregate interactions remain significant above Tm, especially in later stages, potentially forming insoluble aggregates.

Conclusions:

  • Seeded BSA aggregation kinetics are complex, involving both monomer addition and aggregate fusion.
  • Aggregate-aggregate interactions play a critical role, particularly in seeded systems and near Tm.
  • Findings highlight the importance of considering seeding effects for biopharmaceutical shelf-life and accurate spectroscopic analysis.