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Trivalent cation-induced phase separation in proteins: ion specific contribution in hydration also counts
1Department of Chemical, Biological & Macromolecular Sciences, S.N. Bose National Centre for Basic Sciences, Block-JD; Sector-III, Salt Lake, Kolkata-700106, India. rajib@bose.res.in.
Physical Chemistry Chemical Physics : PCCP
|September 23, 2022
Summary
Multivalent ions induce liquid-liquid phase separation (LLPS) in bovine serum albumin by altering water hydration. Trivalent ions specifically trigger LLPS without disrupting protein structure, highlighting the role of hydrophilic hydration.
Area of Science:
- Biophysics
- Protein Chemistry
- Solution Chemistry
Background:
- Multivalent metal ions can induce liquid-liquid phase separation (LLPS) in negatively charged globular proteins.
- Protein aggregation during LLPS is often driven by entropy and solvation effects.
- Understanding the role of hydration in ion-induced LLPS is crucial for protein science.
Purpose of the Study:
- To experimentally investigate the changes in water hydration during ion-induced LLPS of bovine serum albumin (BSA).
- To determine the influence of ion charge on LLPS and associated hydration changes.
- To elucidate the role of hydrophilic hydration in the LLPS mechanism.
Main Methods:
- Fourier Transform Infrared (FTIR) spectroscopy in the Far-Infrared to Terahertz (FIR-THz) range (50–750 cm-1; 1.5–22.5 THz).
- Dynamic Light Scattering (DLS) to confirm aggregate formation.
- Circular Dichroism (CD) spectroscopy to assess protein structural integrity.
Main Results:
- All trivalent ions tested (La3+, Y3+, Ho3+, Al3+) induced LLPS in BSA.
- LLPS was confirmed by DLS, while CD measurements showed no significant perturbation of protein structure.
- THz spectroscopy revealed ion-specific perturbations in water's vibrational modes, correlating with LLPS induction and indicating altered hydration.
Conclusions:
- Trivalent ions effectively induce LLPS in BSA without causing denaturation.
- The observed LLPS is strongly linked to ion-specific changes in water hydration, particularly hydrophilic hydration.
- FTIR-THz spectroscopy is a valuable tool for probing hydration dynamics in protein phase transitions.
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