Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity

Stina Lindman; Iseult Lynch; Eva Thulin; Hanna Nilsson; Kenneth A Dawson; Sara Linse

doi:10.1021/nl062743+

Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity

Stina Lindman, Iseult Lynch, Eva Thulin, Hanna Nilsson, Kenneth A Dawson, Sara Linse

Earth and Environmental Sciences

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

301 Citations (Scopus)

Abstract

Nanoparticles in biological fluids almost invariably become coated with proteins that may confer nanomedical and nanotoxicological effects. Understanding these effects requires quantitative measurements using simple systems. Adsorption of HSA to copolymer nanoparticles of varying hydrophobicity and curvature was studied using ITC, yielding stoichiometry, affinity, and enthalpy changes upon binding. The hydrophobicity was controlled via the co-monomer ratio, N-iso-propylacrylamide/N-tert-butylacrylamide. The most hydrophobic particles become fully covered with a single layer of protein, except at high curvature.

Original language	English
Pages (from-to)	914-20
Number of pages	7
Journal	Nano Letters
Volume	7
Issue number	4
DOIs	https://doi.org/10.1021/nl062743+
Publication status	Published - Apr 2007

Keywords

Acrylamides
Adsorption
Coated Materials, Biocompatible
Computer Simulation
Crystallization
Humans
Hydrophobic and Hydrophilic Interactions
Materials Testing
Models, Chemical
Molecular Conformation
Nanoparticles
Nanotechnology
Particle Size
Protein Binding
Serum Albumin
Surface Properties
Thermodynamics

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10.1021/nl062743+

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title = "Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity",

abstract = "Nanoparticles in biological fluids almost invariably become coated with proteins that may confer nanomedical and nanotoxicological effects. Understanding these effects requires quantitative measurements using simple systems. Adsorption of HSA to copolymer nanoparticles of varying hydrophobicity and curvature was studied using ITC, yielding stoichiometry, affinity, and enthalpy changes upon binding. The hydrophobicity was controlled via the co-monomer ratio, N-iso-propylacrylamide/N-tert-butylacrylamide. The most hydrophobic particles become fully covered with a single layer of protein, except at high curvature.",

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author = "Stina Lindman and Iseult Lynch and Eva Thulin and Hanna Nilsson and Dawson, {Kenneth A} and Sara Linse",

year = "2007",

month = apr,

doi = "10.1021/nl062743+",

language = "English",

volume = "7",

pages = "914--20",

journal = "Nano Letters",

issn = "1530-6984",

publisher = "American Chemical Society",

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T1 - Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity

AU - Lindman, Stina

AU - Lynch, Iseult

AU - Thulin, Eva

AU - Nilsson, Hanna

AU - Dawson, Kenneth A

AU - Linse, Sara

PY - 2007/4

Y1 - 2007/4

N2 - Nanoparticles in biological fluids almost invariably become coated with proteins that may confer nanomedical and nanotoxicological effects. Understanding these effects requires quantitative measurements using simple systems. Adsorption of HSA to copolymer nanoparticles of varying hydrophobicity and curvature was studied using ITC, yielding stoichiometry, affinity, and enthalpy changes upon binding. The hydrophobicity was controlled via the co-monomer ratio, N-iso-propylacrylamide/N-tert-butylacrylamide. The most hydrophobic particles become fully covered with a single layer of protein, except at high curvature.

AB - Nanoparticles in biological fluids almost invariably become coated with proteins that may confer nanomedical and nanotoxicological effects. Understanding these effects requires quantitative measurements using simple systems. Adsorption of HSA to copolymer nanoparticles of varying hydrophobicity and curvature was studied using ITC, yielding stoichiometry, affinity, and enthalpy changes upon binding. The hydrophobicity was controlled via the co-monomer ratio, N-iso-propylacrylamide/N-tert-butylacrylamide. The most hydrophobic particles become fully covered with a single layer of protein, except at high curvature.

KW - Acrylamides

KW - Adsorption

KW - Coated Materials, Biocompatible

KW - Computer Simulation

KW - Crystallization

KW - Humans

KW - Hydrophobic and Hydrophilic Interactions

KW - Materials Testing

KW - Models, Chemical

KW - Molecular Conformation

KW - Nanoparticles

KW - Nanotechnology

KW - Particle Size

KW - Protein Binding

KW - Serum Albumin

KW - Surface Properties

KW - Thermodynamics

U2 - 10.1021/nl062743+

DO - 10.1021/nl062743+

M3 - Article

C2 - 17335269

SN - 1530-6984

VL - 7

SP - 914

EP - 920

JO - Nano Letters

JF - Nano Letters

IS - 4

ER -

Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity

Abstract

Keywords

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