Contact
    Start Publications Temperature-Induced Denaturation of BSA Protein Molecules for ...
    ←  Publication Finder
    QSense

    Temperature-Induced Denaturation of BSA Protein Molecules for Improved Surface Passivation Coatings

    Year: 2018

    Journal: ACS Appl. Mater. Interfaces, Volume 10, SEP 26, page 32047–32057

    Authors: Park, Jae Hyeon; Jackman, Joshua A.; Ferhan, Abdul Rahim; Ma, Gamaliel Junren; Yoon, Bo Kyeong; Cho, Nam-Joon

    Keywords: surface passivation; biofouling; bovine serum albumin; protein adsorption; quartz crystal microbalance-dissipation; localized surface plasmon resonance

    Bovine serum albumin (BSA) is the most widely used protein for surface passivation applications, although it has relatively weak, nonsticky interactions with hydrophilic surfaces such as silica-based materials. Herein, we report a simple and versatile method to increase the stickiness of BSA protein molecules adsorbing onto silica surfaces, resulting in up to a 10-fold improvement in blocking efficiency against serum biofouling. Circular dichroism spectroscopy, dynamic light scattering, and nanoparticle tracking analysis showed that temperature-induced denaturation of BSA proteins in bulk solution resulted in irreversible unfolding and protein oligomerization, thereby converting weakly adhesive protein monomers into a more adhesive oligomeric form. The heat-treated, denatured BSA oligomers remained stable after cooling. Room-temperature quartz crystal microbalance-dissipation and localized surface plasmon resonance experiments revealed that denatured BSA oligomers adsorbed more quickly and in larger mass quantities onto silica surfaces than native BSA monomers. We also determined that the larger surface contact area of denatured BSA oligomers is an important factor contributing to their more adhesive character. Importantly, denatured BSA oligomers were a superior passivating agent to inhibit biofouling on silica surfaces and also improved Western blot application performance. Taken together, the findings demonstrate how temperature-induced denaturation of BSA protein molecules can lead to improved protein-based coatings for surface passivation applications.
    View publication