AVS 46th International Symposium
    Biomaterial Interfaces Group Wednesday Sessions
       Session BI-WeP

Paper BI-WeP2
Protein Nanopatterning on a Gold/Aluminum Nanoarray

Wednesday, October 27, 1999, 5:30 pm, Room 4C

Session: Poster Session
Presenter: C.K. Woods, Duke University
Authors: C.K. Woods, Duke University
Z.-P. Yang, Duke University
A. Chilkoti, Duke University
Correspondent: Click to Email
Protein nanopatterning has potential applications in the fabrication of multianalyte, proximal probe biosensors, genomic arrays, as well as modulation of cell-substrate phenomena. We have developed a technique to immobilize proteins on a surface with spatial resolution of around 100 nm. An ultraflat nanoarray of gold and aluminum is created on a silicon wafer by combining nanosphere lithography with "ultraflat template stripping"- a technique for creating ultraflat thin films of metal. The ultraflat gold/aluminum nanoarray is then incubated in a hexadecanethiol (HDT) solution, which forms a hydrophobic, self-assembled monolayer (SAM) on gold but does not adsorb onto the hydrophilic, native oxide layer on aluminum. We hypothesized that protein adsorption on a HDT-functionalized gold/aluminum nanoarray should occur preferentially on the HDT SAM, thereby allowing proteins to be nanopatterned on the 100 nm gold features. Formation of the HDT SAM on gold but not on aluminum was investigated separately on gold and aluminum substrates using contact angle goniometry, ellipsometry and atomic force microscopy (AFM). The model protein, Ribonuclease A, was found to adsorb preferentially to the HDT SAM on gold with a signal to background ratio of about 6. AFM studies of protein adsorption on HDT-functionalized ultraflat gold/aluminum nanoarrays are currently in progress as are experiments on extending this approach using SAMs presenting biological ligands.