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A Method for Investigation of Size-Dependent Protein Binding to Nanoholes Using Intrinsic Fluorescence of Proteins

Malekian, Bita; Maximov, Ivan LU ; Timm, Rainer LU ; Cedervall, Tommy LU and Hessman, Dan LU (2017) In ACS Omega 2(8). p.4772-4778
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
ACS Omega
volume
2
issue
8
pages
4772 - 4778
publisher
American Chemical Society (ACS)
ISSN
2470-1343
DOI
10.1021/acsomega.7b00241
language
English
LU publication?
yes
id
d7e03b62-2dab-47af-9b9c-ec2b812789bf
alternative location
http://pubs.acs.org/doi/10.1021/acsomega.7b00241
date added to LUP
2018-02-07 17:29:47
date last changed
2018-02-14 13:41:44
@article{d7e03b62-2dab-47af-9b9c-ec2b812789bf,
  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.},
  author       = {Malekian, Bita and Maximov, Ivan and Timm, Rainer and Cedervall, Tommy and Hessman, Dan},
  issn         = {2470-1343},
  language     = {eng},
  month        = {08},
  number       = {8},
  pages        = {4772--4778},
  publisher    = {American Chemical Society (ACS)},
  series       = {ACS Omega},
  title        = {A Method for Investigation of Size-Dependent Protein Binding to Nanoholes Using Intrinsic Fluorescence of Proteins},
  url          = {http://dx.doi.org/10.1021/acsomega.7b00241},
  volume       = {2},
  year         = {2017},
}