Journal of Agricultural and Food Chemistry · 2019 · 89 citations · 29 references
Life SciencesBiochemistryFood ScienceEnzymologyNanomaterialsProtein BiochemistryEnzyme CharacterizationNanoparticle CharacterizationNanoparticle InterfacesPolymeric NanoparticlesProtein Corona FormationProteolytic EnzymesBiomolecule-nanoparticle InteractionsFluorescence QuenchingNanoparticle-biomolecule InteractionsNanoparticlesPolystyreneProtein CoronaUltraviolet-visible Absorption SpectroscopyVan Der Waals Forces
The protein corona (PC), which defines the biological identity of nanoparticles in the blood, is well-known, but no comprehensive and systematic study has been conducted yet on the formation of PCs in the gastrointestinal environment. Thus, this study aimed to explore the interaction between model polystyrene nanoparticles (PS-NPs) of 50-100 nm and three digestive enzymes, namely, pepsin, α-amylase, and trypsin. Results showed that the thicknesses of the PCs formed by α-amylase and trypsin were 25-100 and 50-100 nm, respectively. The zeta-potential values of PS-NPs after incubation significantly increased. The fluorescence quenching and ultraviolet-visible-absorption spectra suggested that interactions between the nanoparticles and the enzymes occurred. Synchronous fluorescence spectra showed that the PS-NPs could induce microenvironmental changes in digestive enzymes. The thermodynamic parameters suggested that the interaction was mainly driven by hydrogen bonds and van der Waals forces.
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Understanding the Kinetics of Protein–Nanoparticle Corona Formation
Oriol Vilanova, Judith J. Mittag, Philip M. Kelly et al. · ACS Nano · 2016 · 283 citations · Full text