Theoretical and Physical Chemistry Institute, National Hellenic Research Foundation, 48 Vassileos Constantinou Avenue, 11635 Athens, Greece.
Jülich Centre for Neutron Science JCNS Forschungszentrum Jülich GmbH, Outstation at Heinz Maier-Leibnitz Zentrum (MLZ), Lichtenbergstraße 1, 85747 Garching, Germany.
Soft Matter. 2018 Apr 18;14(15):2860-2869. doi: 10.1039/C8SM00208H.
The complexation of lysozyme with aggregates from two triblock amphiphilic polyelectrolytes of the same blocks but different topologies and block molar masses, namely PS-b-SCPI-b-PEO and SCPI-b-PS-b-PEO, is investigated by scattering and spectroscopy methods. Light scattering reveals that the interaction with lysozyme causes shrinkage of the self-assembled nanoparticles in the case of the hydrophobic-polyelectrolyte-hydrophilic sequence. In the polyelectrolyte-hydrophobic-hydrophilic sequence, the opposite trend is observed. Small angle neutron scattering confirms the existence of micellar and fractal aggregates and the complexation with lysozyme. The pH-dependence of the interactions and the stability of the hybrid protein/polymer nanoparticles upon salt addition are tested. The native conformation of the protein is found to be preserved during complexation. This study reveals that both micellar and fractal aggregates made of amphiphilic triblock polyelectrolytes are capable of loading with oppositely charged proteins in a controllable manner, tuned primarily by the structure of the triblock terpolymer.
通过散射和光谱方法研究了溶菌酶与两种具有相同嵌段但拓扑结构和嵌段摩尔质量不同的两亲嵌段聚电解质（PS-b-SCPI-b-PEO 和 SCPI-b-PS-b-PEO）的聚集物的络合作用。光散射表明，与溶菌酶相互作用会导致疏水电荷聚合物-亲水电荷聚合物序列中自组装纳米颗粒的收缩。在聚电解质-疏水电荷聚合物-亲水电荷聚合物序列中，观察到相反的趋势。小角中子散射证实了胶束和分形聚集体的存在以及与溶菌酶的络合。测试了相互作用的 pH 依赖性以及盐添加时杂化蛋白/聚合物纳米颗粒的稳定性。发现蛋白质的天然构象在络合过程中得以保留。这项研究表明，由两亲嵌段三嵌段共聚物形成的胶束和分形聚集体都能够以可控的方式装载带相反电荷的蛋白质，主要通过三嵌段共聚物的结构进行调节。
