Phase separation, aggregation, and complexation of triton-X100 and bovine serum albumin mixture: A combined cloud point and UV–visible spectroscopic approaches

• Published in: International journal of biological macromolecules Vol. 269; no. Pt 2; p. 132184
• Main Authors: Bhuiyan, Habiba Akhter, Khan, Javed Masood, Kumar, Dileep, Banjare, Manoj Kumar, Islam, Md. Rafikul, Rana, Shahed, Hoque, Md. Anamul, Rahman, Mohammad Majibur, Kabir, Shariff E.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01-06-2024
• Subjects: Interaction; Protein BSA; Thermodynamic; Interaction; Protein BSA; Thermodynamic
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2024.132184

Phase separation and aggregation behaviour of triton X-100 (TX-100) and bovine serum albumin (BSA) mixture were investigated using cloud point and UV–visible spectroscopic techniques. The effects of various hydrotropes (HYTs) - namely, sodium salicylate (SS), sodium benzoate (SB), glycerol (Glyc), and 4-aminobenzoic acid (4-ABA) - on the cloud point (CP) of TX-100 + BSA were determined. The obtained CP values for the mixed system in the presence of HYTs followed the order:CPH2O+4−ABA<CPH2O+Glyc<CPH2O+SB<CPH2O+SS. The measured critical micellization concentration (CMC) values of the TX-100 + BSA mixture were found to be significantly altered with varying amounts of BSA. The calculated free energy of clouding and micellization indicated the non-spontaneous nature of the phase transition and the spontaneous association of the TX-100 + BSA mixture. The non-spontaneity of phase separation decreased with increasing concentrations of HYTs. The enumerated values of ∆Hco and ∆Sco were consistently recorded as negative and positive magnitudes, respectively, in all aqueous HYTs media. The clouding process occurred due to a combination of hydrophobic and electrostatic interactions. The binding constant of the mixed system was determined employing the UV–vis spectroscopic method using the Benesi-Hildebrand equation.