Probing Adsorption Behaviors of BSA onto Chiral Surfaces of Nanoparticles

Abstract

Chiral properties of nanoscale materials are of importance as they dominate interactions with proteins in physiological environments; however, they have rarely been investigated. In this study, a systematic investigation is conducted for the adsorption behaviors of bovine serum albumin (BSA) onto the chiral surfaces of gold nanoparticles (AuNPs), involving multiple techniques and molecular dynamic (MD) simulation. The adsorption of BSA onto both L- and D-chiral surfaces of AuNPs shows discernible differences involving thermodynamics, adsorption orientation, exposed charges, and affinity. As a powerful supplement, MD simulation provides a molecular-level understanding of protein adsorption onto nanochiral surfaces. Salt bridge interaction is proposed as a major driving force at protein-nanochiral interface interaction. The spatial distribution features of functional groups (COO , NH , and CH ) of chiral molecules on the nanosurface play a key role in the formation and location of salt bridges, which determine the BSA adsorption orientation and binding strength to chiral surfaces. Sequentially, BSA corona coated on nanochiral surfaces affects their uptake by cells. The results enhance the understanding of protein corona, which are important for biological effects of nanochirality in living organisms.

Effects of Nanoparticle Electrostatics and Protein–Protein Interactions on Corona Formation: Conformation and Hydrodynamics

“…Although these results revealed the effect of the protein shape, particle size, and surface properties on the corona formation, most simulations have been performed using a CG model or an implicit‐solvent model, which do not always accurately capture the dynamics and structural change of proteins and their interactions with particles. To overcome this, Shao and Hall, and Wang et al recently performed all‐atom simulations, showing the conformational change of SA protein adsorbed on gold nanoparticles. Tavakol et al's all‐atom and CG simulations showed the effects of glucose and cholesterol on the adsorption of plasma proteins onto PS particles .…”

Room-temperature preparation of a chiral covalent organic framework for the selective adsorption of amino acid enantiomers

“…9,10 Adsorption separation based on porous materials has shown advantages due to their strong chiral recognition ability, longterm stability, and less complexity. 11 The exploration of chiral-functionalized porous materials as adsorbents for the highly efficient resolution of enantiomers has received extensive attention; these materials include metalorganic frameworks, 12,13 porous organic cages, 14,15 metalorganic cages 16,17 and composite porous materials. 18 However, the type of adsorbents for enantioselective adsorption was far more enough due to its challengeable preparation.…”

Modulation of Mesenchymal Stem Cells Mechanosensing at Fluid Interfaces by Tailored Self‐Assembled Protein Monolayers

“…This observation suggests that assembly of BSA at the PFD interface was looser than that at PFTBA. Figure d shows dynamic force microscopy (DFM) images that reveal homogeneous thicknesses of 2.78 ± 0.19 nm and 6.36 ± 0.12 nm for PFD and PFTBA, respectively, which agrees with the theoretical monolayer thickness of serum albumin protein whose diameter is 3–6 nm (albumin is the main component of serum protein) . Also, the low contrast of the images indicates a homogenous surface with root mean square (rms) roughness values within the picometer range (0.62 ± 0.11 nm for PFD and 0.49 ± 0.13 nm for PFTBA).…”