Diverse Role of Buffer Mediums and Protein Concentrations to Mediate the Multimodal Interaction of Phenylalanine-Functionalized Gold Nanoparticle and Lysozyme Protein at Same Nominal pH

Abstract

Recently, buffer molecules have been known to affect intermolecular protein-protein interactions at physiological pH. However, the roles of buffer molecules and different monolayer protein concentrations remain elusive in controlling the interaction of gold nanoparticles (Au NPs) with protein molecules. Herein, for the first time taking phenylalanine functionalized gold nanoparticles (Au-Phe NPs) and lysozyme (Lyz) protein as model systems, we report that buffer molecules of different charges (at a particular pH) play diverse roles in protein-Au NPs interaction, particularly in protein induced Au NPs aggregation. Among different buffers, negatively charged buffer (citrate and phosphate) induces aggregation of both Au-Phe NPs and Lyz protein, whereas zwitterionic and positive buffer (HEPES, MOPS, and Tris) only cause the Au NPs aggregation. Taking the diverse role of buffer into account, we propose multimodal models for stability and protein induced aggregation mechanism of NPs at different monolayer (sub-, near-, and excess) concentrations of Lyz in different medium. © 2024 American Chemical Society.