Instituto de Investigaciones Fisicoquímicas, Teóricas y Aplicadas (INIFTA), UNLP-CONICET, diag. 113 & calle 64, La Plata B1906ZAA, Argentina.
J Phys Chem B. 2024 Jan 11;128(1):371-380. doi: 10.1021/acs.jpcb.3c07283. Epub 2023 Dec 29.
This study explores the impact of network functionalization and chemical composition on the pH-responsive behavior of polymer nanogels and their adsorption of proteins. Using a thermodynamic theory informed by a molecular model, this work evaluates the interactions of three proteins with varying isoelectric points (insulin, myoglobin, and cytochrome c) and pH-responsive nanogels based on methacrylic acid or allylamine motifs. Three different functionalization strategies are considered, with pH-responsive segments distributed randomly, at the center, or on the surface of the polymer network. Our results show that the spatial distribution of functional units affects both the nanogels' mechanical response to pH changes and the level and localization of adsorbed proteins. The dependence of protein adsorption on the salt concentration is also investigated, with the conclusion that it is best to encapsulate proteins at low salt concentrations and aim for release at high salt concentrations. These results provide valuable information for the design of pH-responsive nanogels as vehicles for protein encapsulation, transport, and administration.
本研究探讨了网络功能化和化学成分对聚合物纳米凝胶的 pH 响应行为及其对蛋白质吸附的影响。本工作使用热力学理论和分子模型评估了三种具有不同等电点（胰岛素、肌红蛋白和细胞色素 c）的蛋白质与基于甲基丙烯酸或丙烯胺结构的 pH 响应纳米凝胶之间的相互作用。考虑了三种不同的功能化策略，其中 pH 响应段随机分布、位于中心或聚合物网络表面。我们的结果表明，功能单元的空间分布不仅影响纳米凝胶对 pH 变化的机械响应，还影响吸附蛋白质的水平和位置。还研究了蛋白质吸附对盐浓度的依赖性，得出的结论是最好在低盐浓度下封装蛋白质，并在高盐浓度下进行释放。这些结果为设计作为蛋白质封装、运输和给药载体的 pH 响应纳米凝胶提供了有价值的信息。
