Elucidating How Different Amphipathic Stabilizers Affect BSA Protein Conformational Properties and Adsorption...

Area of Science:

• Biomaterials Science
• Surface Chemistry
• Protein Adsorption

Background:

• Bovine serum albumin (BSA) is widely used in surface coatings and drug delivery.
• Amphipathic stabilizers are crucial for maintaining BSA properties during purification.
• Understanding stabilizer effects on adsorbed BSA is vital for surface coating applications.

Purpose of the Study:

• To investigate the binding interactions between BSA and different amphiphiles (caprylic acid, monocaprylin, methyl caprylate).
• To determine how these interactions affect BSA adsorption behavior and conformational stability on silica surfaces.
• To explore how amphiphile selection influences the properties of BSA adlayers.

Main Methods:

• Systematic investigation of binding interactions between BSA and caprylic acid (CA), monocaprylin (MC), and methyl caprylate (ME) at various molar ratios.
• Analysis of BSA conformational properties in solution and adsorbed states.
• Characterization of BSA adlayer properties, including packing density, on silica surfaces.

Main Results:

• Anionic CA exhibited the highest binding affinity to BSA, enhancing solution stability and reducing adsorption-induced conformational changes, but resulted in lower packing densities.
• Nonionic MC showed moderate binding affinity, stabilizing BSA in both solution and adsorbed states, and facilitating higher packing densities in adlayers.
• Distinct headgroups of amphiphiles significantly influenced BSA binding and subsequent adsorption behavior.

Conclusions:

• The type and concentration of amphipathic stabilizers critically control BSA adsorption and adlayer properties.
• Rational selection of stabilizers can optimize BSA-based surface coatings for specific applications.
• Findings provide insights for designing improved protein-based surface materials.