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

Lindman, Stina LU ; Lynch, Iseult LU ; Thulin, Eva LU ; Nilsson, Hanna LU ; Dawson, Kenneth and Linse, Sara LU (2007) In Nano Letters 7(4). p.914-920
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.
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Nano Letters
volume
7
issue
4
pages
914 - 920
publisher
The American Chemical Society
external identifiers
  • wos:000245600500012
  • scopus:34248155667
ISSN
1530-6992
DOI
10.1021/nl062743+
language
English
LU publication?
yes
id
a6a03451-1912-43e8-98a7-9c0561bad813 (old id 666370)
date added to LUP
2007-12-17 08:31:02
date last changed
2017-11-19 04:04:05
@article{a6a03451-1912-43e8-98a7-9c0561bad813,
  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.},
  author       = {Lindman, Stina and Lynch, Iseult and Thulin, Eva and Nilsson, Hanna and Dawson, Kenneth and Linse, Sara},
  issn         = {1530-6992},
  language     = {eng},
  number       = {4},
  pages        = {914--920},
  publisher    = {The American Chemical Society},
  series       = {Nano Letters},
  title        = {Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity},
  url          = {http://dx.doi.org/10.1021/nl062743+},
  volume       = {7},
  year         = {2007},
}