la8b00944_si_001.docx (5.22 MB)

Ionic Strength-Responsive Binding between Nanoparticles and Proteins

Download (5.22 MB)
journal contribution
posted on 22.06.2018, 00:00 by Xiaohan Wang, Shi Zhang, Yisheng Xu, Xiaotao Zhao, Xuhong Guo
Electrostatic interaction is a strong, dominant nonspecific interaction which was extensively studied in protein–nanoparticle (NP) interactions [Lounis, F. M.; J. Phys. Chem. B 2017, 121, 2684−2694; Tavares, G. M.; Langmuir 2015, 31, 12481–12488; Antonov, M.; Biomacromolecules 2010, 11, 51–59], whereas the role of hydrophobic interaction arising from the abundant hydrophobic residues of globule proteins upon protein–NP binding between the proteins and charged nanoparticles has rarely been studied. In this work, a series of positively charged magnetic nanoparticles (MNPs) were prepared via atom transfer radical polymerization and surface hydrophobicity differentiation was achieved through postpolymerization quaternization by different halohydrocarbons. The ionic strength- and hydrophobicity-responsive binding of these MNPs toward β-lactoglobulin (BLG) was studied by both qualitative and quantitative methods including turbidimetric titration, dynamic light scattering, and isothermal titration calorimetry. Judged from the critical binding pH and binding constant for MNP–BLG complexation, the dependence of binding affinity on surface hydrophobicity exhibited an interesting shift with increasing ionic strength, which means that the MNPs with higher surface hydrophobicity exhibits weaker binding affinity at lower ionic strength but stronger affinity at higher ionic strength. This interesting observation could be attributed to the difference in ionic strength responsiveness for hydrophobic and electrostatic interactions. In this way, the well-tuned binding pattern could be achieved with optimized binding affinity by controlling the surface hydrophobicity of MNPs and ionic strength, thus endowing this system with great potential to fabricate separation and delivery system with high selectivity and efficiency.

History

Exports