Abstract
A complex of physicochemical methods was used to study the aggregation characteristics of an imidazolium-containing amphiphile and its ability for complex formation with bovine serum albumin (BSA). Tensiometry showed that adding BSA to the surfactant decreases the aggregation threshold of the system by a factor of 50. Dynamic light scattering established, that the size of the surfactant–BSA complexes depends on the size of the polypeptide (6–10 nm) and is independent on the concentrations of the surfactant and BSA. The Stern‒Volmer constants and surfactant‒protein binding constants were calculated from fluorescence spectroscopy data.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
