Functional magnetic nanoparticles for protein delivery applications: understanding protein-nanoparticle interactions

Rajat Sharma; Daniel Ungar; Edward Dyson; Stephen Rimmer; Victor Chechik

doi:10.1039/d3nr04544g

Functional magnetic nanoparticles for protein delivery applications: understanding protein-nanoparticle interactions

Rajat Sharma, Daniel Ungar, Edward Dyson, Stephen Rimmer, Victor Chechik

Research output: Contribution to journal › Article › peer-review

Abstract

Iron oxide nanoparticles (IONPs) surface functionalised with thermo-responsive polymers can encapsulate therapeutic proteins and release them upon heating with an alternating magnetic field above the lower critical solution temperature (LCST). In order to make this delivery system clinically-relevant, we prepared IONPs coated with poly-N-isopropylmethacrylamide (PNIPMAM), a polymer with LCST above human body temperature. The optimal polymer chain length and nanoparticle size to achieve LCST of ca. 45 °C were 19 kDa PNIPMAM and 16 nm IONPs. The PNIPMAM-coated IONPs could encapsulate a range of proteins which were released upon heating above LCST in the presence of a competitor protein or serum. A small amount of encapsulated protein leakage was observed below LCST. The efficiency of protein encapsulation and release was correlated with molecular weight and glycosylation state of the proteins. Magnetic heating resulted in a faster protein release as compared to conventional heating without significant temperature increase of the bulk solution.

Original language	English
Number of pages	12
Journal	Nanoscale
Early online date	29 Dec 2024
DOIs	https://doi.org/10.1039/d3nr04544g
Publication status	Accepted/In press - 20 Dec 2023

Bibliographical note

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10.1039/d3nr04544gLicence: CC BY-NC

Functional magnetic nanoparticles for protein delivery applications: understanding protein– nanoparticle interactions
© The Royal Society of Chemistry 2024
Final published version, 1.16 MBLicence: CC BY-NC

Cite this

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title = "Functional magnetic nanoparticles for protein delivery applications: understanding protein-nanoparticle interactions",

abstract = "Iron oxide nanoparticles (IONPs) surface functionalised with thermo-responsive polymers can encapsulate therapeutic proteins and release them upon heating with an alternating magnetic field above the lower critical solution temperature (LCST). In order to make this delivery system clinically-relevant, we prepared IONPs coated with poly-N-isopropylmethacrylamide (PNIPMAM), a polymer with LCST above human body temperature. The optimal polymer chain length and nanoparticle size to achieve LCST of ca. 45 °C were 19 kDa PNIPMAM and 16 nm IONPs. The PNIPMAM-coated IONPs could encapsulate a range of proteins which were released upon heating above LCST in the presence of a competitor protein or serum. A small amount of encapsulated protein leakage was observed below LCST. The efficiency of protein encapsulation and release was correlated with molecular weight and glycosylation state of the proteins. Magnetic heating resulted in a faster protein release as compared to conventional heating without significant temperature increase of the bulk solution.",

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T2 - understanding protein-nanoparticle interactions

AU - Sharma, Rajat

AU - Ungar, Daniel

AU - Dyson, Edward

AU - Rimmer, Stephen

AU - Chechik, Victor

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AB - Iron oxide nanoparticles (IONPs) surface functionalised with thermo-responsive polymers can encapsulate therapeutic proteins and release them upon heating with an alternating magnetic field above the lower critical solution temperature (LCST). In order to make this delivery system clinically-relevant, we prepared IONPs coated with poly-N-isopropylmethacrylamide (PNIPMAM), a polymer with LCST above human body temperature. The optimal polymer chain length and nanoparticle size to achieve LCST of ca. 45 °C were 19 kDa PNIPMAM and 16 nm IONPs. The PNIPMAM-coated IONPs could encapsulate a range of proteins which were released upon heating above LCST in the presence of a competitor protein or serum. A small amount of encapsulated protein leakage was observed below LCST. The efficiency of protein encapsulation and release was correlated with molecular weight and glycosylation state of the proteins. Magnetic heating resulted in a faster protein release as compared to conventional heating without significant temperature increase of the bulk solution.

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