Deciphering BSA adsorption onto COL-BC: Interpretations from statistical physics modeling

Abstract

In this current study, a single-energy double layer model was employed to inspect the adhesion mechanism of bovine serum albumin (BSA) on porous microsphere of cellulose (BC) collagen (COL) bacterium (COL-BC). Six physicochemical variables defining the retention mechanism, :the number of anchored BSA protein per site (n), the amount of (COL-BC) available pores (NM), the capacity of adsorbed quantity (Qa), the specific surface area (As), the concentrations at half saturation (C1/2) and the molar binding energy (ΔE1) are determined. Calculations revealed that n ≥ 1 indicating that an average of one BSA per site is linked to one (COL-BC) receptor site with forming two layers. The BSA/(COL-BC) docking system exhibits a weak binding affinity as evidenced by the computed molar adsorption energy (ΔE1) which is below 40 kJ/mol. This energetic observation aligns with the characteristics of a physical and exothermic binding mechanism. Analysis of the (COL-BC) surface using the Kelvin equation revealed a pore size distribution (PSDs) extending across 0.05 μm–2 μm, providing insights into the stereochemistry of its receptor sites. Discussion of the BSA/COL-BC adhesion reaction through Polanyi equation unveils an adsorption energy distribution (AED) localized between 0 and 15 kJ/mol, consistent with a weak interaction profile characteristic of a physisorption mechanism. Finally, three thermodynamic functions were estimated in order to macroscopically study the BSA/(COL-BC) adsorption systems.This work is involved to provide more information about the adsorption of BSA on the COL-BC microsphere and investigate a theorical approach for the application of the controlled release technology.