Document Detail

Large-area nanopatterning of self-assembled monolayers of alkanethiolates by interferometric lithography.
MedLine Citation:
PMID:  20695609     Owner:  NLM     Status:  MEDLINE    
We demonstrate that interferometric lithography provides a fast, simple approach to the production of patterns in self-assembled monolayers (SAMs) with high resolution over square centimeter areas. As a proof of principle, two-beam interference patterns, formed using light from a frequency-doubled argon ion laser (244 nm), were used to pattern methyl-terminated SAMs on gold, facilitating the introduction of hydroxyl-terminated adsorbates and yielding patterns of surface free energy with a pitch of ca. 200 nm. The photopatterning of SAMs on Pd has been demonstrated for the first time, with interferometric exposure yielding patterns of surface free energy with similar features sizes to those obtained on gold. Gold nanostructures were formed by exposing SAMs to UV interference patterns and then immersing the samples in an ethanolic solution of mercaptoethylamine, which etched the metal substrate in exposed areas while unoxidized thiols acted as a resist and protected the metal from dissolution. Macroscopically extended gold nanowires were fabricated using single exposures and arrays of 66 nm gold dots at 180 nm centers were formed using orthogonal exposures in a fast, simple process. Exposure of oligo(ethylene glycol)-terminated SAMs to UV light caused photodegradation of the protein-resistant tail groups in a substrate-independent process. In contrast to many protein patterning methods, which utilize multiple steps to control surface binding, this single step process introduced aldehyde functional groups to the SAM surface at exposures as low as 0.3 J cm(-2), significantly less than the exposure required for oxidation of the thiol headgroup. Although interferometric methods rely upon a continuous gradient of exposure, it was possible to fabricate well-defined protein nanostructures by the introduction of aldehyde groups and removal of protein resistance in nanoscopic regions. Macroscopically extended, nanostructured assemblies of streptavidin were formed. Retention of functionality in the patterned materials was demonstrated by binding of biotinylated proteins.
J Adams; G Tizazu; Stefan Janusz; S R J Brueck; G P Lopez; G J Leggett
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Langmuir : the ACS journal of surfaces and colloids     Volume:  26     ISSN:  1520-5827     ISO Abbreviation:  Langmuir     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-08-10     Completed Date:  2010-11-22     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9882736     Medline TA:  Langmuir     Country:  United States    
Other Details:
Languages:  eng     Pagination:  13600-6     Citation Subset:  IM    
Department of Chemistry, University of Sheffield, Brook Hill, Sheffield S3 7HF, UK.
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MeSH Terms
Nanostructures / chemistry*
Polyethylene Glycols / chemistry*
Ultraviolet Rays
Reg. No./Substance:
0/Polyethylene Glycols

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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