AVS 49th International Symposium
    Biomaterials Tuesday Sessions
       Session BI+SS-TuA

Paper BI+SS-TuA4
Molecular Recognition Mediated Fabrication of Protein Nanostructures by Dip-Pen Lithography

Tuesday, November 5, 2002, 3:00 pm, Room C-201

Session: Molecular Recognition Surfaces
Presenter: S. Zauscher, Duke University
Authors: J. Hyun, Duke University
S.J. Ahn, Duke University
W. Lee, Duke University
S. Zauscher, Duke University
A. Chilkoti, Duke University
Correspondent: Click to Email
The spatially controlled immobilization of biomolecules on solid surfaces at the nanometer length-scale is driven by the possibility of fabricating new sensors and actuators that will enable detection and actuation at the single molecule level. This communication describes how dip-pen nanolithography (DPN) in combination with the high-affinity streptavidin-biotin, protein-ligand system provides a simple and versatile "bottom-up" approach to create nanoscale biomolecular architectures in a step-wise fashion. This method involves the fabrication of nanoscale features by patterning a self-assembled monolayer (SAM) of a COOH-terminated alkanethiol on a gold substrate by DPN, followed by covalent immobilization of a high-affinity small-molecule ligand (biotin) onto the nanopatterned SAM and subsequent molecular recognition of its protein binding partner (streptavidin) from solution. We fabricated streptavidin nanostructures with lateral feature sizes in the range of 10-400 nm by this method, and have shown that the streptavidin nanopatterns can be used as a template to pattern biotinylated molecules of interest from solution. Because the binding of the final, target molecule is mediated by a highly specific molecular recognition interaction that occurs solely in the patterned region against a non-fouling background, this approach should allow patterning a biomolecule of interest directly from complex mixtures such as cell lysate without purification, which is not possible with alternative DPN methods that involve physisorption or covalent conjugation.