Exploring Protein Corona Formation on Fucoidan-Coated Poly(isobutyl cyanoacrylate) Nanoparticles: Implications for Drug Delivery

High Resolution Image Download MS PowerPoint Slide Serum proteins play an essential role in nanosystems’ stealth properties governing their distribution and targeting to specific sites. Opsonin proteins can induce nanoparticle degradation, elimination, and reduced therapeutic efficiency. The objective is to evaluate how PIBCA nanoparticles coated with fucoidan (NP-Fuc) interact with serum proteins, clarifying their behavior within the body and understanding whether this can impact the in vivo application of these nanoparticles. Static and dynamic interaction studies were carried out with bovine serum albumin (BSA), fetal bovine serum (FBS), and human serum using nanosight, absorption, and fluorescence spectroscopy. Scanning electron microscopy, infrared spectroscopy, and hydrogen nuclear magnetic resonance studies were conducted. Static and dynamic studies showed interaction of NP-Fuc with BSA, evidenced by the increase in nanoparticle size (from 349.5 ± 4.34 nm to 2 μm). Additionally, nanosight analysis also showed the interaction between BSA and NP-Fuc according to the refringence and the hydrodynamic radius (cloud effect) around the nanoparticles. The adsorption technique showed the interaction due to changes in BSA’s absorption and fluorescence profiles. Infrared and 1 H NMR spectra showed the presence of BSA in the NP-Fuc-BSA nanoparticles, indicating the protein binding to nanoparticles. Considering the results, NP-Fuc interacts with BSA to form an NP-Fuc-BSA complex. Further studies are important to optimize the size of NP-Fuc-BSA as a promising nanocarrier for drug release.