“…We examined interactions between pristine PhG NPs and several globular proteins, namely bovine serum albumin (BSA), lysozyme, and globulin (immunoglobulin), being motivated by the similarity in their shapes and dimensions but the difference in peptidic structures and isoelectric points (pI) (Table S1). At pH = 7.4, BSA (pI ∼ 4.7–4.9), lysozyme (pI ∼ 10.5–11.0), and globulin (pI ∼ 7.2) exhibit negative, positive, and neutral charges, respectively, which could provide insights into the nature of PhG NP–protein interactions that were studied using DLS and isothermal titration calorimetry (ITC), the gold standard for the quantitative analysis of intermolecular interactions …”