Thermostability and reversibility of silver nanoparticle–protein binding

Bo Wang, Shane Seabrook, Praveen Nedumpully-Govindan, Pengyu Chen, Hong Yin, Lynne Waddington, V. Epa, David Alan Winkler, Jason Kirby, Feng Ding, Pu Ke

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    Abstract

    The interactions between nanoparticles (NPs) and proteins in living systems are a precursor to the formation of a NP-protein "corona" that underlies cellular and organism responses to nanomaterials. However, the thermodynamic properties and reversibility of NP-protein interactions have rarely been examined. Using an automated, high-throughput and temperature-controlled dynamic light scattering (DLS) technique we observed a distinct hysteresis in the hydrodynamic radius of branched polyethyleneimine (BPEI) coated-silver nanoparticles (bAgNPs) exposed to like-charged lysozyme during the processes of heating and cooling, in contrast to the irreversible interactions between bAgNPs and oppositely charged alpha lactalbumin (ALact). Our discrete molecular dynamics (DMD) simulations offered a new molecular insight into the differential structure, dynamics and thermodynamics of bAgNPs binding with the two protein homologs and further revealed the different roles of the capping agents of citrate and BPEI in NP-protein interactions. This study facilitates our understanding of the transformation of nanomaterials in living systems, whose implications range from the field study of nanotoxicology to nanomaterials synthesis, nanobiotechnology and nanomedicine.

    Original languageEnglish
    Pages (from-to)1728-1739
    Number of pages12
    JournalPhysical Chemistry Chemical Physics
    Volume17
    Issue number3
    DOIs
    Publication statusPublished - 2015

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    Wang, B., Seabrook, S., Nedumpully-Govindan, P., Chen, P., Yin, H., Waddington, L., Epa, V., Winkler, D. A., Kirby, J., Ding, F., & Ke, P. (2015). Thermostability and reversibility of silver nanoparticle–protein binding. Physical Chemistry Chemical Physics, 17(3), 1728-1739. https://doi.org/10.1039/c4cp04996a