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Protein adsorption and complement activation for di-block copolymer nanoparticles

Vauthier, Christine; Persson, Björn LU ; Lindner, Peter and Cabane, Bernard (2011) In Biomaterials 32(6). p.1646-1656
Abstract
Four types of nanoparticles with core-diffuse shell structures have been synthesized through self-assembly of PICBA-Dextran block copolymers. These nanoparticles are designed to carry pharmaceutically active molecules into the human body through injection into the blood stream. In this work, we have determined how the characteristics of the diffuse shell influence the adsorption of three types of proteins: Bovine Serum Albumin (BSA), fibrinogen, and a protein from the complement system that triggers recognition and elimination by macrophages. We have determined the structural characteristics of the diffuse shells using Nuclear Magnetic Resonance (NMR), Small Angle Neutron Scattering (SANS) and Quasi-Elastic Light Scattering (QELS). We have... (More)
Four types of nanoparticles with core-diffuse shell structures have been synthesized through self-assembly of PICBA-Dextran block copolymers. These nanoparticles are designed to carry pharmaceutically active molecules into the human body through injection into the blood stream. In this work, we have determined how the characteristics of the diffuse shell influence the adsorption of three types of proteins: Bovine Serum Albumin (BSA), fibrinogen, and a protein from the complement system that triggers recognition and elimination by macrophages. We have determined the structural characteristics of the diffuse shells using Nuclear Magnetic Resonance (NMR), Small Angle Neutron Scattering (SANS) and Quasi-Elastic Light Scattering (QELS). We have measured the adsorption of Bovine Serum Albumin (BSA) through Immuno-diffusion methods, and found that it adsorbed in substantial amounts even when the distance between dextran chains at the core-diffuse shell interface is quite short. We have observed the aggregation of the nanoparticles induced by fibrinogen, and found that it was prevented when the density of dextran chains protruding from the core surface was sufficiently high. Finally we have measured the activation of the complement system by the nanoparticles, and found that it was also limited by the surface density of dextran chains that protrude from the core and by their mesh size within the diffuse shell. (C) 2010 Elsevier Ltd. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Core-diffuse shell nanoparticles, Mesh size, BSA, Fibrinogen, C3, Adsorption isotherm
in
Biomaterials
volume
32
issue
6
pages
1646 - 1656
publisher
Elsevier
external identifiers
  • wos:000286698100020
  • scopus:78650283439
ISSN
1878-5905
DOI
10.1016/j.biomaterials.2010.10.026
language
English
LU publication?
yes
id
1409ea03-0a05-484d-b8f4-ec3759aa7de0 (old id 1876432)
date added to LUP
2011-04-18 10:33:40
date last changed
2017-11-19 03:17:11
@article{1409ea03-0a05-484d-b8f4-ec3759aa7de0,
  abstract     = {Four types of nanoparticles with core-diffuse shell structures have been synthesized through self-assembly of PICBA-Dextran block copolymers. These nanoparticles are designed to carry pharmaceutically active molecules into the human body through injection into the blood stream. In this work, we have determined how the characteristics of the diffuse shell influence the adsorption of three types of proteins: Bovine Serum Albumin (BSA), fibrinogen, and a protein from the complement system that triggers recognition and elimination by macrophages. We have determined the structural characteristics of the diffuse shells using Nuclear Magnetic Resonance (NMR), Small Angle Neutron Scattering (SANS) and Quasi-Elastic Light Scattering (QELS). We have measured the adsorption of Bovine Serum Albumin (BSA) through Immuno-diffusion methods, and found that it adsorbed in substantial amounts even when the distance between dextran chains at the core-diffuse shell interface is quite short. We have observed the aggregation of the nanoparticles induced by fibrinogen, and found that it was prevented when the density of dextran chains protruding from the core surface was sufficiently high. Finally we have measured the activation of the complement system by the nanoparticles, and found that it was also limited by the surface density of dextran chains that protrude from the core and by their mesh size within the diffuse shell. (C) 2010 Elsevier Ltd. All rights reserved.},
  author       = {Vauthier, Christine and Persson, Björn and Lindner, Peter and Cabane, Bernard},
  issn         = {1878-5905},
  keyword      = {Core-diffuse shell nanoparticles,Mesh size,BSA,Fibrinogen,C3,Adsorption isotherm},
  language     = {eng},
  number       = {6},
  pages        = {1646--1656},
  publisher    = {Elsevier},
  series       = {Biomaterials},
  title        = {Protein adsorption and complement activation for di-block copolymer nanoparticles},
  url          = {http://dx.doi.org/10.1016/j.biomaterials.2010.10.026},
  volume       = {32},
  year         = {2011},
}