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Temperature affects the supramolecular structures resulting from alpha-lactalbumin-lysozyme interaction
Michaël Nigen1, Thomas Croguennec, Denis Renard
1INRA, Agrocampus Rennes, UMR 1253, Science & Technologie du Lait et de l'Oeuf, 65 rue de Saint Brieuc, F-35000 Rennes, France.
Lysozyme interacts with calcium-depleted alpha-lactalbumin (apo alpha-LA), forming temperature-dependent supramolecular structures like aggregates and coacervates. These protein assemblies highlight the role of unfolding intermediates in protein-driven assembly.
Area of Science:
- Protein interactions
- Biophysical chemistry
- Supramolecular chemistry
Background:
- Alpha-lactalbumin and lysozyme are homologous globular proteins with opposite charges.
- Understanding protein interactions is key to biomolecular assembly.
Purpose of the Study:
- Investigate the interaction between alpha-lactalbumin and lysozyme.
- Characterize temperature-dependent supramolecular structures formed by these proteins.
Main Methods:
- Isothermal titration calorimetry (ITC) to assess binding.
- Temperature variation to induce and observe structural changes.
Main Results:
- Lysozyme binds to calcium-depleted alpha-lactalbumin (apo alpha-LA), not native alpha-lactalbumin.
- Amorphous aggregates form at 5°C, while coacervate-like droplets form at 45°C.
- Coacervate formation is equimolar, influenced by protein ratio; structures exhibit temperature-dependent stability and coalescence.
Conclusions:
- Protein-protein interactions can yield diverse supramolecular structures.
- Temperature-induced conformational changes in apo alpha-LA are crucial for assembly.
- Alpha-lactalbumin unfolding intermediates play a vital role in protein-driven assembly.
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