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Fabrication of corona-free nanoparticles with tunable hydrophobicity.

Moyano DF, Saha K, Prakash G, Yan B, Kong H, Yazdani M, Rotello VM - ACS Nano (2014)

Bottom Line: A protein corona is formed at the surface of nanoparticles in the presence of biological fluids, masking the surface properties of the particle and complicating the relationship between chemical functionality and biological effects.We present here a series of zwitterionic NPs of variable hydrophobicity that do not adsorb proteins at moderate levels of serum protein and do not form hard coronas at physiological serum concentrations.These particles provide platforms to evaluate nanobiological behavior such as cell uptake and hemolysis dictated directly by chemical motifs at the nanoparticle surface.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry, University of Massachusetts Amherst , 710 North Pleasant Street, Amherst, Massachusetts 01003, United States.

ABSTRACT
A protein corona is formed at the surface of nanoparticles in the presence of biological fluids, masking the surface properties of the particle and complicating the relationship between chemical functionality and biological effects. We present here a series of zwitterionic NPs of variable hydrophobicity that do not adsorb proteins at moderate levels of serum protein and do not form hard coronas at physiological serum concentrations. These particles provide platforms to evaluate nanobiological behavior such as cell uptake and hemolysis dictated directly by chemical motifs at the nanoparticle surface.

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(a) Reversible adsorption of proteins and formation of irreversible hard corona over the NP surface. (b) Structures of the nonfouling NPs, along with TEG, NP+, and NP– controls. The ligand structure consists of a hydrophobic interior that confers stability to the NP core, an oligo(ethylene glycol) chain used as a first layer for biocompatibility, and the zwitterionic headgroups to confer ultrafouling properties. The zwitterionic headgroups (the NP surface) differ only in their hydrophobicity, whose relative values can be estimated by the calculated log P of the terminal functionality. (c) Correlation of the calculated log P with toluene/water interfacial tension.
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fig1: (a) Reversible adsorption of proteins and formation of irreversible hard corona over the NP surface. (b) Structures of the nonfouling NPs, along with TEG, NP+, and NP– controls. The ligand structure consists of a hydrophobic interior that confers stability to the NP core, an oligo(ethylene glycol) chain used as a first layer for biocompatibility, and the zwitterionic headgroups to confer ultrafouling properties. The zwitterionic headgroups (the NP surface) differ only in their hydrophobicity, whose relative values can be estimated by the calculated log P of the terminal functionality. (c) Correlation of the calculated log P with toluene/water interfacial tension.

Mentions: Surface functionalization of nanoparticles (NPs) is an essential tool to modulate the behavior of these materials both in vitro and in vivo.1,2 The biodistribution,3 toxicity,4 and clearance5,6 of nanomaterials can be regulated through controlled chemical modifications. However, when NPs are exposed to biofluids, such as plasma or serum, proteins and other biomolecules adsorb on the surface of these materials (Figure 1a).7−9 This in situ formation of a “protein corona”10,11 masks the engineered functionalities on the nanoparticle surfaces, dramatically changing the nature of their interaction with biosystems.12−14 For example, the targeting efficacy of antibody-functionalized NPs are compromised due to the high levels of opsonization.15,16 Likewise, the study of correlations between surface functionality and biological activity is challenging, as the results are subject to the interplay between the chemical moieties and the corona, rather than depending on the functionalities themselves.17,18


Fabrication of corona-free nanoparticles with tunable hydrophobicity.

Moyano DF, Saha K, Prakash G, Yan B, Kong H, Yazdani M, Rotello VM - ACS Nano (2014)

(a) Reversible adsorption of proteins and formation of irreversible hard corona over the NP surface. (b) Structures of the nonfouling NPs, along with TEG, NP+, and NP– controls. The ligand structure consists of a hydrophobic interior that confers stability to the NP core, an oligo(ethylene glycol) chain used as a first layer for biocompatibility, and the zwitterionic headgroups to confer ultrafouling properties. The zwitterionic headgroups (the NP surface) differ only in their hydrophobicity, whose relative values can be estimated by the calculated log P of the terminal functionality. (c) Correlation of the calculated log P with toluene/water interfacial tension.
© Copyright Policy - editor-choice
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4215884&req=5

fig1: (a) Reversible adsorption of proteins and formation of irreversible hard corona over the NP surface. (b) Structures of the nonfouling NPs, along with TEG, NP+, and NP– controls. The ligand structure consists of a hydrophobic interior that confers stability to the NP core, an oligo(ethylene glycol) chain used as a first layer for biocompatibility, and the zwitterionic headgroups to confer ultrafouling properties. The zwitterionic headgroups (the NP surface) differ only in their hydrophobicity, whose relative values can be estimated by the calculated log P of the terminal functionality. (c) Correlation of the calculated log P with toluene/water interfacial tension.
Mentions: Surface functionalization of nanoparticles (NPs) is an essential tool to modulate the behavior of these materials both in vitro and in vivo.1,2 The biodistribution,3 toxicity,4 and clearance5,6 of nanomaterials can be regulated through controlled chemical modifications. However, when NPs are exposed to biofluids, such as plasma or serum, proteins and other biomolecules adsorb on the surface of these materials (Figure 1a).7−9 This in situ formation of a “protein corona”10,11 masks the engineered functionalities on the nanoparticle surfaces, dramatically changing the nature of their interaction with biosystems.12−14 For example, the targeting efficacy of antibody-functionalized NPs are compromised due to the high levels of opsonization.15,16 Likewise, the study of correlations between surface functionality and biological activity is challenging, as the results are subject to the interplay between the chemical moieties and the corona, rather than depending on the functionalities themselves.17,18

Bottom Line: A protein corona is formed at the surface of nanoparticles in the presence of biological fluids, masking the surface properties of the particle and complicating the relationship between chemical functionality and biological effects.We present here a series of zwitterionic NPs of variable hydrophobicity that do not adsorb proteins at moderate levels of serum protein and do not form hard coronas at physiological serum concentrations.These particles provide platforms to evaluate nanobiological behavior such as cell uptake and hemolysis dictated directly by chemical motifs at the nanoparticle surface.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry, University of Massachusetts Amherst , 710 North Pleasant Street, Amherst, Massachusetts 01003, United States.

ABSTRACT
A protein corona is formed at the surface of nanoparticles in the presence of biological fluids, masking the surface properties of the particle and complicating the relationship between chemical functionality and biological effects. We present here a series of zwitterionic NPs of variable hydrophobicity that do not adsorb proteins at moderate levels of serum protein and do not form hard coronas at physiological serum concentrations. These particles provide platforms to evaluate nanobiological behavior such as cell uptake and hemolysis dictated directly by chemical motifs at the nanoparticle surface.

Show MeSH
Related in: MedlinePlus