Impact of oppositely charged shell and cores on interaction of core-shell colloids with differently charged proteins as a route for tuning of the colloids cytotoxicity

Abstract

The present work represents interactions between the core-shell nanoparticles and different proteins, exemplified by lysozyme (LSZ), pepsin, bovine serum albumin (BSA), thioredoxin (TRX) and yellow fluorescent protein (YFP). The core-shell morphology derives from the non-covalent deposition of polyethyleneimine (PEI) onto nanoprecipitated luminescent complex (AuCl)₂L (L is cyclic PNNP ligand). Analysis of the data obtained by DLS, CD spectroscopy, luminescence derived from both (AuCl)₂L and YFP reveal the electrostatically driven interaction of negatively charged proteins with the shell of PEI-(AuCl)₂L. The fluorescence of YFP enables to reveal the inclusion of the protein molecules into the shell. The lack of any luminescent response of PEI-(AuCl)₂L on TRX conforms its electrostatically driven interactions with the shell which, in turn, excludes a binding of the exposed thiol moieties with (AuCl)₂L. The negatively charged surface of pepsin provides the greatest recharging of the PEI-based shell versus the other proteins, which is followed by the enhanced luminescence of (AuCl)₂L. The significant effect of PEI-(AuCl)₂L on the CD spectra of LSZ followed by the decreased intensity of (AuCl)₂L-based luminescence points to specific interaction mode of PEI-(AuCl)₂L with LSZ. The flow cytometry and fluorescent microscopy measurements revealed efficient internalization of PEI-(AuCl)₂L into the Wi-38 cell samples resulting in the efficient staining of all cell organelles. The concentration dependent cytotoxicity of PEI-(AuCl)₂L is detectably enhanced by LSZ, which is correlated with its interaction mode with the nanoparticles.

Keywords: Au(I) complex; Cell internalization; Core-shell nanoparticles; Cytotoxicity; Luminescence; Proteins.