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Temperature-induced aggregation behavior in bovine pancreas trypsin solutions
Sofia Trampari1, Aristeidis Papagiannopoulos2, Stergios Pispas2
1School of Applied Mathematical and Physical Sciences Physics Department, NTUA Zografou Campus, GR, 15780, Greece; Theoretical and Physical Chemistry Institute, National Hellenic Research Foundation, 48 Vassileos Constantinou Avenue, 11635, Athens, Greece.
Biochemical and Biophysical Research Communications
|June 2, 2019
Summary
Increasing temperature non-reversibly enhances Bovine Pancreas Trypsin (BPT) aggregation in aqueous solutions. This protein unfolding and aggregation, driven by hydrophobic exposure, is crucial for developing protein-based nanodrugs.
Area of Science:
- Biochemistry
- Protein Chemistry
- Materials Science
Background:
- Bovine Pancreas Trypsin (BPT) is a widely used enzyme.
- Understanding BPT behavior under thermal stress is critical for its applications.
- Protein aggregation can impact therapeutic efficacy and formulation stability.
Purpose of the Study:
- To investigate the effects of temperature treatment on BPT in aqueous solutions.
- To elucidate the molecular mechanisms underlying BPT aggregation.
- To provide insights for optimizing thermal treatment protocols for BPT-based nanomedicines.
Main Methods:
- Dynamic, static, and electrophoretic light scattering.
- Fluorescence spectroscopy.
- Circular dichroism.
Main Results:
- BPT aggregation increases non-reversibly with temperature, influenced by pH and salt content.
- Protein unfolding, indicated by tryptophan exposure, correlates with aggregation.
- Aggregate surface charge is intensified and dominated by negative residues.
Conclusions:
- Thermal treatment induces irreversible BPT aggregation via hydrophobic interior exposure.
- Findings are valuable for developing thermal treatment protocols for BPT in nanodrug manufacturing.
- Controlled thermal processing can potentially be used to engineer BPT properties for nanomedicine.
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