2020
DOI: 10.1039/d0ma00188k
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Pore structure and particle shape modulates the protein corona of mesoporous silica particles

Abstract:

The hard and soft protein corona of mesoporous silica particles and its integrity is significantly affected by their morphology, with spherical particles offering a homogenous protein coating which results in enhanced cellular uptake.

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Cited by 5 publications
(2 citation statements)
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“…Apart from nanoparticle size, morphology, and shape, pore structures have also been determined as a factor to influence adsorbed protein numbers and composition on MSNs, resulting in higher proportions of low molecular weight (MW) proteins. 22 Additionally, using a set of porous nanoparticles bearing the same well-defined shape and size but differing in pore diameter, Vidaurre-Agut et al demonstrated a distinct effect of pore diameter on competitive serum protein adsorption using a representative low MW protein (apolipoprotein A-II) and a high MW protein (complement C3). 23 More specifically, the extent of protein adsorption was comparatively evaluated on dense nonporous silica nanoparticles ("SNPs") with a diameter of ∼120 nm, standard MSNs with a hexagonally ordered pore structure and a pore diameter of 2.7 nm, and large-pore silica ("LPS") nanoparticles with increasing pore diameters of 4.8, 6.2, 7.4, and 14 nm.…”
Section: Chemical Signatures Of the Proteinmentioning
confidence: 99%
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“…Apart from nanoparticle size, morphology, and shape, pore structures have also been determined as a factor to influence adsorbed protein numbers and composition on MSNs, resulting in higher proportions of low molecular weight (MW) proteins. 22 Additionally, using a set of porous nanoparticles bearing the same well-defined shape and size but differing in pore diameter, Vidaurre-Agut et al demonstrated a distinct effect of pore diameter on competitive serum protein adsorption using a representative low MW protein (apolipoprotein A-II) and a high MW protein (complement C3). 23 More specifically, the extent of protein adsorption was comparatively evaluated on dense nonporous silica nanoparticles ("SNPs") with a diameter of ∼120 nm, standard MSNs with a hexagonally ordered pore structure and a pore diameter of 2.7 nm, and large-pore silica ("LPS") nanoparticles with increasing pore diameters of 4.8, 6.2, 7.4, and 14 nm.…”
Section: Chemical Signatures Of the Proteinmentioning
confidence: 99%
“…In addition, molecular dynamics (MD) simulations identified salt bridge formation as a driving force in protein–chiral surface interactions, where the spatial distribution of surface-exposed functional groups (−COO – , −NH 3 + , and −CH 3 ) of penicillamine determined the formation and location of the salt bridges that defined the orientation of the adsorbed BSA and subsequent nanoparticle cell uptake. Apart from nanoparticle size, morphology, and shape, pore structures have also been determined as a factor to influence adsorbed protein numbers and composition on MSNs, resulting in higher proportions of low molecular weight (MW) proteins . Additionally, using a set of porous nanoparticles bearing the same well-defined shape and size but differing in pore diameter, Vidaurre-Agut et al demonstrated a distinct effect of pore diameter on competitive serum protein adsorption using a representative low MW protein (apolipoprotein A-II) and a high MW protein (complement C3) .…”
Section: Chemical Signatures Of the Protein Coronamentioning
confidence: 99%