Understanding the nano-bio interactions using real-time surface plasmon resonance tool.

Area of Science:

• Biophysics
• Nanotechnology
• Materials Science

Background:

• Understanding nano-bio interfaces is crucial but limited.
• Surface plasmon resonance (SPR) is underutilized for nanoparticle (NP) protein binding kinetics.
• Nanoparticle surface properties critically affect biological interactions.

Purpose of the Study:

• To investigate nanoparticle-protein interactions at the nano-bio interface.
• To elucidate the influence of NP surface charge on protein binding kinetics using SPR.
• To compare interactions of charged NPs with model proteins at physiological pH.

Main Methods:

• Utilized surface plasmon resonance (SPR) for real-time kinetic analysis.
• Employed biophysical characterization techniques to study NP-protein interactions.
• Investigated interactions between poly lactic-co-glycolic acid (PLGA) NPs (negative) and chitosan oligosaccharide (COS)-coated PLGA NPs (positive) with bovine serum albumin (BSA) and lysozyme (LYZ).

Main Results:

• SPR revealed significant differences in binding affinity and kinetics.
• Both NP types showed much greater affinity for positively charged lysozyme (LYZ) compared to negatively charged bovine serum albumin (BSA).
• Adsorption studies corroborated the SPR findings regarding NP-protein affinity.

Conclusions:

• Nanoparticle surface properties, beyond net charge, dominate protein interactions.
• SPR is a valuable tool for characterizing nano-bio interactions.
• This research enhances the biophysical understanding of nano-bio interfaces.