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
| Autor: | Mattias Berglin, Yi Yang, Hans Elwing, Karin Fromell, Kristina Nilsson Ekdahl, Bo Nilsson |
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| Rok vydání: | 2017 |
| Předmět: |
Conformational change
Protein Denaturation Flexibility (anatomy) Protein Conformation Biophysics General Physics and Astronomy 02 engineering and technology Complement factor I 010402 general chemistry Physical Chemistry 01 natural sciences General Biochemistry Genetics and Molecular Biology Biomaterials Contact angle chemistry.chemical_compound Adsorption Polymer chemistry medicine General Materials Science Fysikalisk kemi chemistry.chemical_classification Factor XII Acrylate Chemistry General Chemistry Polymer Complement C3 021001 nanoscience & nanotechnology Biofysik 0104 chemical sciences medicine.anatomical_structure Acrylates Tissue Adhesives 0210 nano-technology Protein Binding |
| Zdroj: | Biointerphases. 12(2) |
| ISSN: | 1559-4106 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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