Polyacrylic acids-bovine serum albumin complexation: Structure and dynamics

Area of Science:

• Biochemistry
• Polymer Science
• Physical Chemistry

Background:

• Bovine serum albumin (BSA) is a key protein in biological systems.
• Polyacrylic acids are synthetic polymers with diverse applications.
• Understanding protein-polyelectrolyte interactions is crucial for biomaterial development.

Purpose of the Study:

• To investigate the complexation behavior of BSA with polyacrylic acids across varying pH.
• To characterize the structural and dynamic properties of BSA-polyacrylic acid complexes.
• To elucidate the influence of pH on complexation regimes and phase diagrams.

Main Methods:

• Turbidimetry
• Dynamic Light Scattering (DLS)
• Zeta-potential measurements
• Nuclear Magnetic Resonance (NMR)
• Computational electrostatic potential determination

Main Results:

• Identified two distinct complexation regimes: weak and strong, dependent on pH and polymer mass.
• Characterized pH-induced changes in complex structure, properties, and dynamics.
• NMR and computational methods provided insights into constituent dynamics and binding interactions.

Conclusions:

• The study refines the interpretation of the BSA-polyacrylic acid phase diagram.
• pH is a critical factor modulating the electrostatic interactions and binding modes.
• The findings contribute to understanding polyelectrolyte complex formation and behavior.