| Autor: |
Zhang X, Firkowska-Boden I, Arras MML; Large Scale Structures Group, Neutron Scattering Division , Oak Ridge National Laboratory , Oak Ridge , Tennessee 37831 , United States., Kastantin MJ; Department of Chemical and Biological Engineering , University of Colorado Boulder , Boulder , Colorado 80309 , United States., Helbing C, Özogul A, Gnecco E, Schwartz DK; Department of Chemical and Biological Engineering , University of Colorado Boulder , Boulder , Colorado 80309 , United States., Jandt KD; Jena Center for Soft Matter (JCSM) , Friedrich Schiller University Jena , Philosophenweg 7 , 07743 Jena , Germany. |
| Jazyk: |
angličtina |
| Zdroj: |
Langmuir : the ACS journal of surfaces and colloids [Langmuir] 2018 Nov 27; Vol. 34 (47), pp. 14309-14316. Date of Electronic Publication: 2018 Nov 09. |
| DOI: |
10.1021/acs.langmuir.8b02917 |
| Abstrakt: |
Surface nanostructures are increasingly more employed for controlled protein assembly on functional nanodevices, in nanobiotechnology, and in nanobiomaterials. However, the mechanism and dynamics of how nanostructures induce order in the adsorbed protein assemblies are still enigmatic. Here, we use single-molecule mapping by accumulated probe trajectories and complementary atomic force microscopy to shed light on the dynamic of in situ assembly of human plasma fibrinogen (HPF) adsorbed on nanostructured polybutene-1 (PB-1) and nanostructured polyethylene (PE) surfaces. We found a distinct lateral heterogeneity of HPF-polymer nanostructure interface (surface occupancy, residence time, and diffusion coefficient) that allow identifying the interplay between protein topographical nanoconfinement, protein diffusion mechanism, and ordered protein self-assembly. The protein diffusion analysis revealed high-diffusion polarization without correlation to the anisotropic friction characteristic of the polymer surfaces. This suggests that HPF molecules confined on the nanosized PB-1 needle crystals and PE shish-kebab crystals, respectively, undergo partial detachment and diffuse via a Sansetsukon-like nanocrawling mechanism. This mechanism is based on the intrinsic flexibility of HPF in the coiled-coil regions. We conclude that nanostructured surfaces that encourage this characteristic surface mobility are more likely to lead to the formation of ordered protein assemblies and may be useful for advanced nanobiomaterials. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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