Bovine serum albumin and tiagabine binding dynamics in complex coacervate core micelles
Er, Serpil Turan, Bayraktutan, Omer Faruk, Bayraktutan, Tugba
This research aimed to attain encapsulation that maintains stability at physiological pH utilizing complex coacervate core micelles (C3Ms) with bovine serum albumin (BSA) protein, and to assess the impact of this encapsulation on binding dynamics. To achieve this, C3Ms were created utilizing cationic PVPEVB (poly 4vinylpyridine-co-ethylvinylbenzene) and anionic PSS (poly sodium 4-styrenesulfonate) polymers. The binding kinetics of bovine serum albumin (BSA) with the antiepileptic medication tiagabine sulfate (TGB) were examined utilizing the Stern-Volmer equation. The C3Ms enhance the interaction between BSA and TGB, resulting in a more robust or efficient binding compared to a standard buffer solution. The binding in C3Ms led to the creation of a more stable complex. Conformational changes in BSA during protein-drug interactions in C3Ms were characterized using circular dichroism spectra (CD), synchronous fluorescence, and 3D fluorescence spectra. Encapsulation properties were evaluated through dynamic light scattering (DLS) measurements and transmission electron microscopy (TEM) imagery. This research clarified the binding dynamics of BSA and TGB during encapsulation in C3Ms and the alterations to these dynamics.
- Journal
- REACTIVE & FUNCTIONAL POLYMERS
- Year
- 2025
- Volume
- 215
- ISSN
- 1381-5148
- eISSN
- 1873-166X
- DOI
- 10.1016/j.reactfunctpolym.2025.106360
- WoS UID
- WOS:001507023200001