How the surface charge of the nanoparticles modulates their protein and cell interactions?
Saad Megahed a b, Nicole Wutke c, Neus Feliu b, Markus Klapper c, Wolfgang Parak b
a Physics Department, Faculty of Science, Al-Azhar University, 11884 Cairo, Egypt
b Fachbereich Physik, CHyN, Universität Hamburg, 22761 Hamburg, Germany
c Max Planck Institute for polymer Research, 55128 Mainz, Germany
Proceedings of Advanced materials and devices for nanomedicine (AMA4MED)
VALÈNCIA, Spain, 2022 May 3rd - 4th
Organizers: Claudia Tortiglione and María Moros
Contributed talk, Saad Megahed, presentation 003
DOI: https://doi.org/10.29363/nanoge.amamed.2022.003
Publication date: 22nd April 2022

Colloidal Nanoparticles (NPs) have great potential in many applications including biological applications. The biomedical application efficacy of the NPs is determined and limited by different parameters, such as the formation of protein corona upon the interaction of the NPs with the biological milieu. Which in some cases negatively influences their final fate and reduces their circulation time. There are already different strategies aiming to suppress or at least minimize the effect of the protein corona. In the current work, we have developed a universal surface modification method based on amphiphilic polymers to modify the surface charge of the NPs from positive, negative, and zwitterionic charges, while keeping the same surface chemistry. In addition to that, studying their protein and cell interactions versus different surface charges. The physicochemical characterization of the NPs has been studied using different methods such as Dynamic light scattering (DLS), Zeta potential (ζ), UV-Vis spectroscopy, and Drop shape analyzer. The protein-NPs adsorption has been studied using Fluorescence Correlation Spectroscopy (FCS) to evaluate the change in the overall hydrodynamic size of the NPs upon interaction with different protein concentrations. Furthermore, their cellular interactions, in terms of biocompatibility and cellular uptake, have been studied using Flow cytometer and ICP-MS techniques. We have found that the protein adsorption is charge-dependent as well as the cellular uptake, regardless of the size and type of the core. Moreover, the zwitterionic structure showed significant suppression of the protein corona formation, and our results suggest the orientation and nature of the zwitterionic ligand play a major role in such suppression effect. 

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