Asymmetrical interactions between nanoparticles and proteins arising from deformation upon adsorption to surfaces

Biophys Chem. 2023 Aug 23;302:107098. doi: 10.1016/j.bpc.2023.107098. Online ahead of print.ABSTRACTDrug release from polymeric nanoparticles (NPs) is governed by their adsorption onto cell membranes and transmigration across cell walls. These steps are influenced by their interactions with proteins near the cells. These interactions were investigated by studying the sequential adsorption of plasma proteins, albumin (Alb) and fibrinogen (Fg), and micellar NPs using quartz crystal microbalance with dissipation (QCMD), X-ray photoelectron spectroscopy (XPS), and small-angle X-ray scattering (SAXS). The three NPs in the study all have poly(ethylene glycol) (PEG) shells but different cores: amorphous poly(propylene oxide) (PPO), crystalline polycaprolactone (PCL), and poly(desaminotyrosyl-tyrosine octyl ester-co-suberic acid) (DTO-SA). None of the NPs adsorbed onto a pre-adsorbed Fg layer. On the other hand, when the deposition sequence was reversed, Fg was adsorbed onto DTO-SA NP and PCL NP surfaces, but not onto the PPO NP surface. The interactions with Alb were different: DTO-SA did not adsorb onto Alb and vice versa; PPO NP adsorbed onto an Alb layer, but Alb did not adsorb onto the PPO NP layer; and PCL NP reversibly adsorbed onto Alb, but Alb displaced pre-adsorbed PCL NP. Thus, in most instances, the adsorption behavior was asymmetric in that it was dependent on the order of arrival of the adsorbates at the substrate. SAXS data did not show evidence for complex formation i...
Source: Biophysical Chemistry - Category: Chemistry Authors: Source Type: research