Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility
Uppsala University, Sweden.
Goteborg University, Sweden.
Linnaeus University, Sweden.
Linnaeus University, Sweden.
Show others and affiliations
2017 (English)In: Biointerphases, ISSN 1934-8630, E-ISSN 1559-4106, Vol. 12, no 2, 02D417Article in journal (Refereed) Published
Abstract [en]

In previous investigations, the authors have examined the adsorption of albumin, immunoglobulin, and fibrinogen to a series of acrylate polymers with different backbone and side-group flexibility. The authors showed that protein adsorption to acrylates with high flexibility, such as poly(lauryl methacrylate) (PLMA), tends to preserve native conformation. In the present study, the authors have continued this work by examining the conformational changes that occur during the binding of complement factor 3 (C3) and coagulation factor XII (FXII). Native C3 adsorbed readily to all solid surfaces tested, including a series of acrylate surfaces of varying backbone flexibility. However, a monoclonal antibody recognizing a "hidden" epitope of C3 (only exposed during C3 activation or denaturation) bound to the C3 on the rigid acrylate surfaces or on polystyrene (also rigid), but not to C3 on the flexible PLMA, indicating that varying degrees of conformational change had occurred with binding to different surfaces. Similarly, FXII was activated only on the rigid poly(butyl methacrylate) surface, as assessed by the formation of FXIIa-antithrombin (AT) complexes; in contrast, it remained in its native form on the flexible PLMA surface. The authors also found that water wettability hysteresis, defined as the difference between the advancing and receding contact angles, was highest for the PLMA surface, indicating that a dynamic change in the interface polymer structure may help protect the adsorbed protein from conformational changes and denaturation.

Place, publisher, year, edition, pages
2017. Vol. 12, no 2, 02D417
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-30900DOI: 10.1116/1.4985698Scopus ID: 2-s2.0-85021073944OAI: oai:DiVA.org:ri-30900DiVA: diva2:1138621
Note

 Funding details: VR, Vetenskapsrådet; Funding text: The authors wish to thank Deborah McClellan for much appreciated editorial assistance and the authors appreciate Pentti Tengvall for valuable discussions during the preparation of this work. This work was supported by grants from the European Community's Seventh Framework Program under Grant Agreement No. 602699 (DIREKT), the Swedish Research Council (VR), and faculty grants from the Linnaeus University.

Available from: 2017-09-06 Created: 2017-09-06 Last updated: 2017-09-06Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textScopushttp://avs.scitation.org/doi/pdf/10.1116/1.4985698
By organisation
Chemistry, Materials and Surfaces
In the same journal
Biointerphases
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
v. 2.27.0