Multi-parametric surface plasmon resonance platform for studying liposome-serum interactions and protein corona formation

Publication year: 2016
Authors: Otto K. Kari 1, Tatu Rojalin 2, Stefano Salmaso 3, Michela Barattin 4, Hanna Jarva 5, Seppo Meri 6, Marjo Yliperttula 7, Tapani Viitala 8, Arto Urtti 9
Affiliations:

1, 2, 8 - Centre for Drug Research and Division of Pharmaceutical Biosciences, Faculty of Pharmacy, University of Helsinki, Finland
3, 4 - Department of Pharmaceutical and Pharmacological Sciences, University of Padova, Italy
5, 6 - 
Department of Bacteriology and Immunology, Immunobiology Research Program, Faculty of Medicine, and HUSLAB, Division of Clinical Microbiology, Finland
7 - 
Centre for Drug Research and Division of Pharmaceutical Biosciences, Faculty of Pharmacy, University of Helsink, Finland, and Department of Pharmaceutical and Pharmacological Sciences, University of Padova, Italy
9 - 
Centre for Drug Research and Division of Pharmaceutical Biosciences, Faculty of Pharmacy, University of Helsinki, Finland and School of Pharmacy, University of Eastern Finland, Finland

Published in: Drug Delivery and Translational Research, p. 1-13
doi: 10.1007/s13346-016-0320-0

When nanocarriers are administered into the blood circulation, a complex biomolecular layer known as the “protein corona” associates with their surface. Although the drivers of corona formation are not known, it is widely accepted that this layer mediates biological interactions of the nanocarrier with its surroundings. Label-free optical methods can be used to study protein corona formation without interfering with its dynamics. We demonstrate the proof-of-concept for a multi-parametric surface plasmon resonance (MP-SPR) technique in monitoring the formation of a protein corona on surface-immobilized liposomes subjected to flowing 100 % human serum. We observed the formation of formulation-dependent “hard” and “soft” coronas with distinct refractive indices, layer thicknesses, and surface mass densities. MP-SPR was also employed to determine the affinity (KD) of a complement system molecule (C3b) with cationic liposomes with and without polyethylene glycol. Tendency to create a thick corona correlated with a higher affinity of opsonin C3b for the surface. The label-free platform provides a fast and robust preclinical tool for tuning nanocarrier surface architecture and composition to control protein corona formation.


MP-SPR keywords: 100% serum, complement system protein affinity, crude sample, Drug delivery, innate immune system resonses, liposome-serum interactions, nanocarrier surface, opsoninin C3b binding, protein corona formation, refractive index, surface mass densities, surface-immobilized liposomes, thickness