Hydrophobization of bovine serum albumin with cationic surfactants with different hydrophobic chain length

Investigation of bovine serum albumin-surfactant aggregation and its physicochemical characteristics

“…Although the importance of the interaction between proteins and surfactants has been realized since long, nonetheless the fundamental understanding of the molecular mechanisms underlying both the protein-surfactant interactions and role of these interactions in various applications are still moderately understood [7,8]. Mostly, electrostatic interaction and hydrophobic association are the two main driving forces that account for the protein-surfactant interactions [9,10].However, the comprehensive understanding of the mechanism of the organization, size, and micropolarity of the protein-surfactant organized assemblies and the nature of the interfaces are crucial parameters that need to be investigated in addition to the prevailing interactions to orient the protein-surfactant interactions suitable for desired applications.…”

BSA/polyelectrolyte core–shell nanoparticles for controlled release of encapsulated ibuprofen

“…The BSA has a positive charge at this pH so the surface needs 20 ml of PSS to compensate the positive charge. The calculated specific charge of the neutral charge state was 1.42 mequiv./g BSA, which value shows close resemblance with previous experiments [28]. Finally, positively charged Chit (0.3%, pH = 3, in 4, v% acetic acid) was added to the BSA/PSS core-shell nanoparticles.…”

Functionalized gold nanoparticles for 2-naphthol binding and their fluorescence properties

“…The samples were measured after 1 hour of adsorption time. The fluorescence quenching ratio was calculated by using the following equation: 1 − I/I 0 [16][17][18]. The Stern-Volmer equation was used to quantify the differences in quenching efficiency for different kind of analytes as follows:…”