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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 universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Klinisk immunologi.
Gothenburg Univ, Dept Chem & Mol Biol, S-40530 Gothenburg, Sweden..
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Klinisk immunologi. Linnaeus Univ, Linnaeus Ctr Biomat Chem, S-39182 Kalmar, Sweden..
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Klinisk immunologi. Linnaeus Univ, Linnaeus Ctr Biomat Chem, S-39182 Kalmar, Sweden..ORCID-id: 0000-0003-0057-2730
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2017 (engelsk)Inngår i: Biointerphases, ISSN 1934-8630, E-ISSN 1559-4106, Vol. 12, nr 2, 02D417Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
2017. Vol. 12, nr 2, 02D417
HSV kategori
Identifikatorer
URN: urn:nbn:se:uu:diva-329705DOI: 10.1116/1.4985698ISI: 000404045100001PubMedID: 28637352OAI: oai:DiVA.org:uu-329705DiVA: diva2:1147353
Forskningsfinansiär
EU, FP7, Seventh Framework Programme, 602699Swedish Research Council
Tilgjengelig fra: 2017-10-05 Laget: 2017-10-05 Sist oppdatert: 2017-10-05bibliografisk kontrollert

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