Surface-dependent conformations of human plasma fibronectin adsorbed to silica, mica, and hydrophobic surfaces, studied with use of Atomic Force Microscopy
2003 (engelsk)Inngår i: Journal of biomedical materials research. Part A., ISSN 0021-9304, Vol. 64, nr 2, s. 349-356Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]
Human plasma fibronectin (Fn) is a large flexible protein stabilized by intermolecular ionic interactions forming a compact structure. On altering solution conditions, the structure can revert to a more expanded state, thereby exposing previously hidden domains (e.g., cell-binding sites). Electron microscopy images of Fn air-sprayed onto mica surfaces show elongated protein structures, indicating a surface-induced structural change. This makes it interesting to investigate the influence of surface properties on the structure of adsorbed Fn. We have used intermittent-contact Atomic Force Microscopy to investigate the structure of Fn adsorbed onto mica, silica, and methylated silica surfaces. We observed that on silica surfaces, which is hydrophilic, most (70%) of the molecules had an elongated structure with partial intramolecular chain interactions, compare to molecules adsorbed on hydrophobic, methylated surfaces, where a compact structure predominated (70%). On mica surfaces, both compact and elongated protein structures were observed, with a slight preference for the elongated form (53%). Results show that surface physical properties influence the molecular structure of fibronectin on adsorption, which could provide useful information in understanding surface-induced in vivo responses.
sted, utgiver, år, opplag, sider
2003. Vol. 64, nr 2, s. 349-356
Emneord [en]
Absorption, Aluminum Silicates, Fibronectins/*chemistry/ultrastructure, Microscopy; Atomic Force, Models; Molecular, Protein Conformation, Research Support; Non-U.S. Gov't, Silicon Dioxide, Surface Properties
HSV kategori
Identifikatorer
URN: urn:nbn:se:mdh:diva-1840DOI: 10.1002/jbm.a.10423ISI: 000182423200018PubMedID: 12522822Scopus ID: 2-s2.0-0042008055OAI: oai:DiVA.org:mdh-1840DiVA, id: diva2:114503
2006-03-092006-03-092015-07-06bibliografisk kontrollert