Hirun Namon, Kraisit Pakorn, Soontaranon Siriwat
Thammasat University Research Unit in Smart Materials and Innovative Technology for Pharmaceutical Applications (SMIT-Pharm), Faculty of Pharmacy, Thammasat University, Pathumthani 12120, Thailand.
Synchrotron Light Research Institute (Public Organization), Nakhon Ratchasima 30000, Thailand.
Polymers (Basel). 2023 May 26;15(11):2465. doi: 10.3390/polym15112465.
The combination of the thermoresponsive polymer and protein has demonstrated great promise in its applications in drug delivery and tissue engineering fields. This study described the impact of bovine serum albumin (BSA) on the micellization and sol-gel transition behaviors of poloxamer 407 (PX). The micellization of aqueous PX solutions with and without BSA was examined using isothermal titration calorimetry. In the calorimetric titration curves, the pre-micellar region, the transition concentration region, and the post-micellar region were observed. The presence of BSA had no noticeable impact on critical micellization concentration, but the inclusion of BSA caused the pre-micellar region to expand. In addition to studying the self-organization of PX at a particular temperature, the temperature-induced micellization and gelation of PX were also explored using differential scanning calorimetry and rheology. The incorporation of BSA had no discernible effect on critical micellization temperature (CMT), but it did affect gelation temperature (T) and gel integrity of PX-based systems. The response surface approach illustrated the linear relation between the compositions and the CMT. The major factor affecting the CMT of the mixtures was the concentration of PX. The alteration of the T and the gel integrity were discovered to be a consequence of the intricate interaction between PX and BSA. BSA mitigated the inter-micellar entanglements. Hence, the addition of BSA demonstrated a modulating influence on T and a softening effect on gel integrity. Understanding the influence of serum albumin on the self-assembly and gelation of PX will enable the creation of thermoresponsive drug delivery and tissue engineering systems with controlled gelation temperatures and gel strength.
热响应性聚合物与蛋白质的结合在药物递送和组织工程领域的应用中展现出了巨大的前景。本研究描述了牛血清白蛋白（BSA）对泊洛沙姆407（PX）胶束化和溶胶-凝胶转变行为的影响。使用等温滴定量热法研究了含和不含BSA的PX水溶液的胶束化过程。在量热滴定曲线中，观察到了胶束前区域、转变浓度区域和胶束后区域。BSA的存在对临界胶束浓度没有显著影响，但加入BSA导致胶束前区域扩大。除了研究特定温度下PX的自组装，还使用差示扫描量热法和流变学探索了PX的温度诱导胶束化和凝胶化。BSA的加入对临界胶束化温度（CMT）没有明显影响，但它确实影响了基于PX的体系的凝胶化温度（T）和凝胶完整性。响应面法说明了组成与CMT之间的线性关系。影响混合物CMT的主要因素是PX的浓度。发现T和凝胶完整性的改变是PX与BSA之间复杂相互作用的结果。BSA减轻了胶束间的缠结。因此，加入BSA对T表现出调节作用，对凝胶完整性表现出软化作用。了解血清白蛋白对PX自组装和凝胶化的影响将有助于创建具有可控凝胶化温度和凝胶强度的热响应性药物递送和组织工程系统。
