AI Article Synopsis

  • Bovine serum albumin (BSA) is a useful substance in tissue engineering and pharmaceutical research, derived from cattle blood.
  • This study investigated how different polyols affect the phase separation of a mixture of Triton X-100 (TX-100) and BSA, finding that polyols significantly lower the cloud point (CP) of the mixture, with solubility varying based on the type of polyol used.
  • Results indicated that electrostatic forces are dominant at lower concentrations of polyols, while higher concentrations shift interactions to hydrophobic forces; molecular docking confirmed hydrogen bonds and hydrophobic interactions between TX-100 and BSA.

Article Abstract

Bovine serum albumin (BSA) is widely used in tissue engineering and pharmaceutical research. It is readily available as a byproduct of the cattle industry, and collected from blood. In this study, we conducted a physicochemical investigation of the phase separation in a mixture of Triton X-100 (TX-100) and BSA, influenced by various polyols, using the well-established cloud point (CP) determination method. The addition of polyols resulted in a significant reduction in CP values for the TX-100 + BSA mixture. The magnitudes of CP in the experimental system were highly varied with different polyols and followed the order of: [Formula: see text] Under identical conditions, the system exhibited maximum solubility in the xylose solution and minimum solubility in the maltose solution. The positive ΔG values were acquired in all working medium imply the nonspontaneity of phase transition in the TX-100 + BSA system. At lower polyol contents, the negative values of standard enthalpy (∆H) and standard entropy (∆S) changes were observed, suggesting that electrostatic forces dominated as the driving force for clouding. At highest employed polyols concentration in some case, the positive values for ∆H and ∆S were achieved, which indicated that hydrophobic interactions likely dominate the phase partitioning of the amphiphile and protein mixture. Additionally, entropy-enthalpy compensation parameters were calculated and analyzed with a rational approach. Molecular docking analysis further demonstrated the presence of hydrogen bonds and hydrophobic interactions between TX-100 and BSA.

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Source
http://dx.doi.org/10.1016/j.ijbiomac.2024.135298DOI Listing

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