Formation of complexes in aqueous solutions of amphiphilic triblock polyelectrolytes of different topologies and an oppositely charged protein†,Soft Matter

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Formation of complexes in aqueous solutions of amphiphilic triblock polyelectrolytes of different topologies and an oppositely charged protein†
Soft Matter ( IF 2.9 ) Pub Date : 2018-03-06 00:00:00 , DOI: 10.1039/c8sm00208h
Aristeidis Papagiannopoulos _{1,

2,

3,

4} , Maria Karayianni _{1,

2,

3,

4} , Stergios Pispas _{1,

2,

3,

4} , Aurel Radulescu _{5,

6,

7,

8}

Affiliation

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.

中文翻译：

在具有不同拓扑结构的两亲性三嵌段聚电解质和带相反电荷的蛋白质的水溶液中形成配合物†

溶菌酶与来自相同嵌段但拓扑不同和嵌段摩尔质量的两个三嵌段两亲聚电解质的聚集体的络合，即PS- b -SCPI- b -PEO和SCPI- b -PS- b-PEO，通过散射和光谱法研究。光散射表明，在疏水-聚电解质-亲水序列的情况下，与溶菌酶的相互作用导致自组装纳米颗粒的收缩。在聚电解质-疏水-亲水序列中，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。测试了添加盐后相互作用的pH依赖性和杂合蛋白/聚合物纳米颗粒的稳定性。发现该蛋白质的天然构象在复合过程中得以保留。

更新日期：2018-03-06

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