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Inhibition of complement activation on a model biomaterial surface by streptococcal M protein-derived peptides

Engberg, Anna E.; Sandholm, Kerstin; Bexborn, Fredrik; Persson, Jenny J LU ; Nilsson, Bo; Lindahl, Gunnar LU and Ekdahl, Kristina N. (2009) In Biomaterials 30(13). p.2653-2659
Abstract
The aim of this study was to evaluate a new approach to inhibit complement activation triggered by biomaterial surfaces in contact with blood. In order to inhibit complement activation initiated by the classical pathway (CP), we used streptococcal M protein-derived peptides that specifically bind human C4BP, an inhibitor of the CP. The peptides were used to coat polystyrene microtiter wells which served as a model biomaterial. The ability of coated peptides to bind C4BP and to attenuate complement activation via the CP (monitored as generation of fluid-phase C3a and binding of fragments of C3 and C4 to the surface) was investigated using diluted normal human serum, where complement activation by the AP is minimal, as well as serum from a... (More)
The aim of this study was to evaluate a new approach to inhibit complement activation triggered by biomaterial surfaces in contact with blood. In order to inhibit complement activation initiated by the classical pathway (CP), we used streptococcal M protein-derived peptides that specifically bind human C4BP, an inhibitor of the CP. The peptides were used to coat polystyrene microtiter wells which served as a model biomaterial. The ability of coated peptides to bind C4BP and to attenuate complement activation via the CP (monitored as generation of fluid-phase C3a and binding of fragments of C3 and C4 to the surface) was investigated using diluted normal human serum, where complement activation by the AP is minimal, as well as serum from a patient lacking alternative pathway activation. Complement activation (all parameters) was significantly decreased in serum incubated in well surfaces coated with peptides. Total inhibition of complement activation was obtained at peptide coating concentrations as low as 1-5 mu g/mL. Successful use of Streptococcus-derived peptides shows that it is feasible to control complement activation at a model biomaterial surface by capturing autologous complement regulatory molecules from plasma. (C) 2009 Elsevier Ltd. All rights reserved. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
test, In vitro, C4b-binding protein (C4BP), Blood compatibility, Complement, Regulator of complement activation (RCA), Streptococcal M proteins
in
Biomaterials
volume
30
issue
13
pages
2653 - 2659
publisher
Elsevier
external identifiers
  • wos:000264691200026
  • scopus:60849084562
ISSN
1878-5905
DOI
10.1016/j.biomaterials.2009.01.001
language
English
LU publication?
yes
id
391229d3-0c2e-4300-a91d-e57c32af71da (old id 1401195)
date added to LUP
2009-06-15 09:43:32
date last changed
2017-01-01 05:12:09
@article{391229d3-0c2e-4300-a91d-e57c32af71da,
  abstract     = {The aim of this study was to evaluate a new approach to inhibit complement activation triggered by biomaterial surfaces in contact with blood. In order to inhibit complement activation initiated by the classical pathway (CP), we used streptococcal M protein-derived peptides that specifically bind human C4BP, an inhibitor of the CP. The peptides were used to coat polystyrene microtiter wells which served as a model biomaterial. The ability of coated peptides to bind C4BP and to attenuate complement activation via the CP (monitored as generation of fluid-phase C3a and binding of fragments of C3 and C4 to the surface) was investigated using diluted normal human serum, where complement activation by the AP is minimal, as well as serum from a patient lacking alternative pathway activation. Complement activation (all parameters) was significantly decreased in serum incubated in well surfaces coated with peptides. Total inhibition of complement activation was obtained at peptide coating concentrations as low as 1-5 mu g/mL. Successful use of Streptococcus-derived peptides shows that it is feasible to control complement activation at a model biomaterial surface by capturing autologous complement regulatory molecules from plasma. (C) 2009 Elsevier Ltd. All rights reserved.},
  author       = {Engberg, Anna E. and Sandholm, Kerstin and Bexborn, Fredrik and Persson, Jenny J and Nilsson, Bo and Lindahl, Gunnar and Ekdahl, Kristina N.},
  issn         = {1878-5905},
  keyword      = {test,In vitro,C4b-binding protein (C4BP),Blood compatibility,Complement,Regulator of complement activation (RCA),Streptococcal M proteins},
  language     = {eng},
  number       = {13},
  pages        = {2653--2659},
  publisher    = {Elsevier},
  series       = {Biomaterials},
  title        = {Inhibition of complement activation on a model biomaterial surface by streptococcal M protein-derived peptides},
  url          = {http://dx.doi.org/10.1016/j.biomaterials.2009.01.001},
  volume       = {30},
  year         = {2009},
}