The Library
Oxidation of tertiary amine-derivatized surfaces to control protein adhesion
Tools
Dobrzanska, Dorota A., Cooper, A. (Amy), Dowson, Christopher G., Evans, Stephen D., Fox, David J., Johnson, Benjamin R., Biggs, Caroline I., Randev, Rajan, Stec, Helena M., Taylor, Paul C. and Marsh, Andrew (2013) Oxidation of tertiary amine-derivatized surfaces to control protein adhesion. Langmuir, Volume 29 (Number 9). pp. 2961-2970. doi:10.1021/la4003719 ISSN 0743-7463.
|
Text (Final version before changes at proof stage)
WRAP_Marsh_Langmuir_29Jan2013.pdf - Accepted Version Download (1556Kb) | Preview |
Official URL: http://dx.doi.org/10.1021/la4003719
Abstract
Selective oxidation of omega-tertiary amine self-assembled thiol monolayers to tertiary amine N-oxides is shown to transform the adhesion of model proteins lysozyme and fibrinogen upon them. Efficient preparation of both secondary and tertiary linker amides as judged by X-ray photoelectron spectroscopy (XPS) and water droplet contact angle was achieved with an improved amide bond formation on gold quartz crystal microbalance (QCM) sensors using 2-(1H-7-azabenzotriazol-1-yl)-1,1,3,3-tetramethyl hexafluorophosphate methanaminium uronium (HATU). Oxidation with hydrogen peroxide was similarly assessed, and adhesion of lysozyme and fibrinogen from phosphate buffered saline was then assayed by QCM and imaged by AFM. Tertiary amine-functionalized sensors adsorbed multilayers of aggregated lysozyme, whereas tertiary amine N-oxides and triethylene glycol-terminated monolayers are consistent with small protein aggregates. The surface containing a dimethylamine N-oxide headgroup and ethyl secondary amide linker showed the largest difference in adsorption of both proteins. Oxidation of tertiary amine decorated surfaces therefore holds the potential for selective deposition of proteins and cells through masking and other patterning techniques.
Item Type: | Journal Article | ||||
---|---|---|---|---|---|
Subjects: | Q Science > QD Chemistry T Technology > TP Chemical technology |
||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) |
||||
Library of Congress Subject Headings (LCSH): | Self-assembly (Chemistry), Cell adhesion molecules, Proteins, Amphiphiles, Amines -- Oxidation | ||||
Journal or Publication Title: | Langmuir | ||||
Publisher: | American Chemical Society | ||||
ISSN: | 0743-7463 | ||||
Official Date: | 5 March 2013 | ||||
Dates: |
|
||||
Volume: | Volume 29 | ||||
Number: | Number 9 | ||||
Page Range: | pp. 2961-2970 | ||||
DOI: | 10.1021/la4003719 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access | ||||
Copyright Holders: | American Chemical Society | ||||
Date of first compliant deposit: | 24 December 2015 | ||||
Date of first compliant Open Access: | 24 December 2015 | ||||
Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Perry Foundation (UK), Nuffield Foundation (NF), Engineering and Physical Sciences Research Council (EPSRC) |
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |
Downloads
Downloads per month over past year