Protein adsorption and complement activation for di-block copolymer nanoparticles
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1876432
- author
- Vauthier, Christine ; Persson, Björn LU ; Lindner, Peter and Cabane, Bernard
- organization
- publishing date
- 2011
- 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
- pmid:21093043
- ISSN
- 1878-5905
- DOI
- 10.1016/j.biomaterials.2010.10.026
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
- id
- 1409ea03-0a05-484d-b8f4-ec3759aa7de0 (old id 1876432)
- date added to LUP
- 2016-04-01 10:50:09
- date last changed
- 2023-01-02 08:19:36
@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}},
keywords = {{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}},
doi = {{10.1016/j.biomaterials.2010.10.026}},
volume = {{32}},
year = {{2011}},
}