Facile co-assembly process to generate core-shell nanoparticles with functional protein corona

Nisaraporn Suthiwangcharoen, Tao Li, Laying Wu, Heidi B. Reno, Preston Thompson, Qian Wang

Research output: Contribution to journalArticleResearchpeer-review

28 Citations (Scopus)

Abstract

A simple and robust protocol to maintain the structural feature of polymer-protein core-shell nanoparticles (PPCS-NPs) is developed based on the synergistic interactions between proteins and functional polymers. Using the self-assembly method, a broad range of proteins can be assembled to the selective water-insoluble polymers containing pyridine groups. The detailed analysis of the PPCS-NPs structure was conducted using FESEM and thin-sectioned TEM. The results illustrated that the protein molecules are located on the corona of the PPCS-NPs. While proteins are displacing between water and polymer to minimize the interfacial energy, the polymer offers a unique microenvironment to maintain protein structure and conformation. The proposed mechanism is based on a fine balance between hydrophobicity and hydrophilicity, as well as hydrogen bonding between proteins and polymer. The PPCS-NPs can serve as a scaffold to incorporate both glucose oxidase (GOX) and horseradish peroxidase (HRP) onto a single particle. Such a GOX-HRP bienzymatic system showed a ∼20% increase in activity in comparison to the mixed free enzymes. Our method therefore provides a unique platform to preserve protein structure and conformation and can be extended to a number of biomolecules.

Original languageEnglish
Pages (from-to)948-956
Number of pages9
JournalBiomacromolecules
Volume15
Issue number3
DOIs
StatePublished - 10 Mar 2014

Fingerprint

Nanoparticles
Proteins
Polymers
Glucose Oxidase
Glucose oxidase
Horseradish Peroxidase
Conformations
Protein Corona
Functional polymers
Water
Hydrophilicity
Biomolecules
Scaffolds (biology)
Hydrophobicity
Interfacial energy
Scaffolds
Pyridine
Self assembly
Hydrogen bonds
Enzymes

Cite this

Suthiwangcharoen, Nisaraporn ; Li, Tao ; Wu, Laying ; Reno, Heidi B. ; Thompson, Preston ; Wang, Qian. / Facile co-assembly process to generate core-shell nanoparticles with functional protein corona. In: Biomacromolecules. 2014 ; Vol. 15, No. 3. pp. 948-956.
@article{7534c2a31ad6428f92de29373be46f1c,
title = "Facile co-assembly process to generate core-shell nanoparticles with functional protein corona",
abstract = "A simple and robust protocol to maintain the structural feature of polymer-protein core-shell nanoparticles (PPCS-NPs) is developed based on the synergistic interactions between proteins and functional polymers. Using the self-assembly method, a broad range of proteins can be assembled to the selective water-insoluble polymers containing pyridine groups. The detailed analysis of the PPCS-NPs structure was conducted using FESEM and thin-sectioned TEM. The results illustrated that the protein molecules are located on the corona of the PPCS-NPs. While proteins are displacing between water and polymer to minimize the interfacial energy, the polymer offers a unique microenvironment to maintain protein structure and conformation. The proposed mechanism is based on a fine balance between hydrophobicity and hydrophilicity, as well as hydrogen bonding between proteins and polymer. The PPCS-NPs can serve as a scaffold to incorporate both glucose oxidase (GOX) and horseradish peroxidase (HRP) onto a single particle. Such a GOX-HRP bienzymatic system showed a ∼20{\%} increase in activity in comparison to the mixed free enzymes. Our method therefore provides a unique platform to preserve protein structure and conformation and can be extended to a number of biomolecules.",
author = "Nisaraporn Suthiwangcharoen and Tao Li and Laying Wu and Reno, {Heidi B.} and Preston Thompson and Qian Wang",
year = "2014",
month = "3",
day = "10",
doi = "10.1021/bm401819x",
language = "English",
volume = "15",
pages = "948--956",
journal = "Biomacromolecules",
issn = "1525-7797",
publisher = "American Chemical Society",
number = "3",

}

Suthiwangcharoen, N, Li, T, Wu, L, Reno, HB, Thompson, P & Wang, Q 2014, 'Facile co-assembly process to generate core-shell nanoparticles with functional protein corona', Biomacromolecules, vol. 15, no. 3, pp. 948-956. https://doi.org/10.1021/bm401819x

Facile co-assembly process to generate core-shell nanoparticles with functional protein corona. / Suthiwangcharoen, Nisaraporn; Li, Tao; Wu, Laying; Reno, Heidi B.; Thompson, Preston; Wang, Qian.

In: Biomacromolecules, Vol. 15, No. 3, 10.03.2014, p. 948-956.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Facile co-assembly process to generate core-shell nanoparticles with functional protein corona

AU - Suthiwangcharoen, Nisaraporn

AU - Li, Tao

AU - Wu, Laying

AU - Reno, Heidi B.

AU - Thompson, Preston

AU - Wang, Qian

PY - 2014/3/10

Y1 - 2014/3/10

N2 - A simple and robust protocol to maintain the structural feature of polymer-protein core-shell nanoparticles (PPCS-NPs) is developed based on the synergistic interactions between proteins and functional polymers. Using the self-assembly method, a broad range of proteins can be assembled to the selective water-insoluble polymers containing pyridine groups. The detailed analysis of the PPCS-NPs structure was conducted using FESEM and thin-sectioned TEM. The results illustrated that the protein molecules are located on the corona of the PPCS-NPs. While proteins are displacing between water and polymer to minimize the interfacial energy, the polymer offers a unique microenvironment to maintain protein structure and conformation. The proposed mechanism is based on a fine balance between hydrophobicity and hydrophilicity, as well as hydrogen bonding between proteins and polymer. The PPCS-NPs can serve as a scaffold to incorporate both glucose oxidase (GOX) and horseradish peroxidase (HRP) onto a single particle. Such a GOX-HRP bienzymatic system showed a ∼20% increase in activity in comparison to the mixed free enzymes. Our method therefore provides a unique platform to preserve protein structure and conformation and can be extended to a number of biomolecules.

AB - A simple and robust protocol to maintain the structural feature of polymer-protein core-shell nanoparticles (PPCS-NPs) is developed based on the synergistic interactions between proteins and functional polymers. Using the self-assembly method, a broad range of proteins can be assembled to the selective water-insoluble polymers containing pyridine groups. The detailed analysis of the PPCS-NPs structure was conducted using FESEM and thin-sectioned TEM. The results illustrated that the protein molecules are located on the corona of the PPCS-NPs. While proteins are displacing between water and polymer to minimize the interfacial energy, the polymer offers a unique microenvironment to maintain protein structure and conformation. The proposed mechanism is based on a fine balance between hydrophobicity and hydrophilicity, as well as hydrogen bonding between proteins and polymer. The PPCS-NPs can serve as a scaffold to incorporate both glucose oxidase (GOX) and horseradish peroxidase (HRP) onto a single particle. Such a GOX-HRP bienzymatic system showed a ∼20% increase in activity in comparison to the mixed free enzymes. Our method therefore provides a unique platform to preserve protein structure and conformation and can be extended to a number of biomolecules.

UR - http://www.scopus.com/inward/record.url?scp=84896766331&partnerID=8YFLogxK

U2 - 10.1021/bm401819x

DO - 10.1021/bm401819x

M3 - Article

VL - 15

SP - 948

EP - 956

JO - Biomacromolecules

JF - Biomacromolecules

SN - 1525-7797

IS - 3

ER -