Simenido Georgii A, Zubanova Ekaterina M, Ksendzov Evgenii A, Kostjuk Sergei V, Timashev Peter S, Golubeva Elena N
Faculty of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia.
Research Institute for Physical Chemical Problems of the Belarusian State University, 220006 Minsk, Belarus.
Polymers (Basel). 2024 May 9;16(10):1335. doi: 10.3390/polym16101335.
The influence of bovine serum albumin (BSA) on collapsing poly(-isopropylacrylamide) (PNIPAM) chains was studied with turbidimetry and spin probe and spin label electron paramagnetic resonance spectroscopy. An increased ratio of collapsed chains in aqueous solutions in the narrow temperature region near the LCST appeared in the presence of 2.5-10 wt% BSA. The spin probe EPR data indicate that the inner cavities of the BSA dimers are probably responsive to the capture of small hydrophobic or amphiphilic molecules, such as TEMPO nitroxyl radical. The observed features of the structure and dynamics of inhomogeneities of aqueous PNIPAM-BSA solutions, including their mutual influence on the behavior of the polymer and protein below the LCST, should be considered when developing and investigating PNIPAM-based drug delivery systems.
采用比浊法、自旋探针和自旋标记电子顺磁共振波谱研究了牛血清白蛋白（BSA）对聚（N-异丙基丙烯酰胺）（PNIPAM）塌陷链的影响。在2.5-10 wt% BSA存在下，在接近最低临界溶液温度（LCST）的狭窄温度区域内，水溶液中塌陷链的比例增加。自旋探针电子顺磁共振数据表明，BSA二聚体的内腔可能对捕获小的疏水性或两亲性分子（如TEMPO硝基自由基）有响应。在开发和研究基于PNIPAM的药物递送系统时，应考虑观察到的PNIPAM-BSA水溶液不均匀性的结构和动力学特征，包括它们在LCST以下对聚合物和蛋白质行为的相互影响。
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