A Method for Investigation of Size-Dependent Protein Binding to Nanoholes Using Intrinsic Fluorescence of Proteins
(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:
https://lup.lub.lu.se/record/d7e03b62-2dab-47af-9b9c-ec2b812789bf
- author
- Malekian, Bita
; Maximov, Ivan
LU
; Timm, Rainer LU
; Cedervall, Tommy LU and Hessman, Dan LU
- organization
- publishing date
- 2017-08-31
- type
- Contribution to journal
- publication status
- published
- subject
- in
- ACS Omega
- volume
- 2
- issue
- 8
- pages
- 4772 - 4778
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:30023730
- scopus:85063352443
- ISSN
- 2470-1343
- DOI
- 10.1021/acsomega.7b00241
- language
- English
- LU publication?
- yes
- id
- d7e03b62-2dab-47af-9b9c-ec2b812789bf
- date added to LUP
- 2018-02-07 17:29:47
- date last changed
- 2024-10-14 21:30:07
@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 = {{The 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}}, doi = {{10.1021/acsomega.7b00241}}, volume = {{2}}, year = {{2017}}, }