ArticleACS omega2017
A Method for Investigation of Size-Dependent Protein Binding to Nanoholes Using Intrinsic Fluorescence of Proteins.
Article in ACS omega, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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0 citing papers in PubMed, 3 citations in OpenAlex.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have developed a novel method to study the influence of surface nanotopography on human fibrinogen adsorption at a given surface chemistry. Well-ordered arrays of nanoholes with different diameters down to 45 nm and a depth of 50 nm were fabricated in silicon by electron beam lithography and reactive ion etching. The nanostructured chip was used as a model system to understand the effect of size of the nanoholes on fibrinogen adsorption. Fluorescence imaging, using the intrinsic fluorescence of proteins, was used to characterize the effect of the nanoholes on fibrinogen adsorption. Atomic force microscopy was used as a complementary technique for further characterization of the interaction. The results demonstrate that as the size of the nanoholes is reduced to 45 nm, fibrinogen adsorption is significantly increased.
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Registered trials
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