AVS 51st International Symposium
    Biomaterial Interfaces Tuesday Sessions
       Session BI+NS-TuM

Paper BI+NS-TuM5
Capture and Release of Proteins on the Nanoscale by Surface-Confined Biomolecular Switches

Tuesday, November 16, 2004, 9:40 am, Room 210D

Session: The Nano-Bio Interface
Presenter: S. Zauscher, Duke University
Authors: J. Hyun, Seoul National University, Korea
W.K. Lee, Duke University
N. Nath, Duke University
A. Chilkoti, Duke University
S. Zauscher, Duke University
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In this paper we describe the fabrication and characterization of stimulus-responsive elastin-like polypeptide (ELP) nanostructures grafted onto -substituted thiolates that were patterned onto gold surfaces by dip-pen nanolithography (DPN). We exploited the hydrophilic-hydrophobic phase transition of ELP in response to a change in ionic strength as a switch in order to reversibly immobilize a thioredoxin-ELP fusion protein onto the ELP nanopattern above the lower critical solution temperature. We demonstrated the biological activity of the Trx-ELP nanoarray by binding an anti-thioredoxin monoclonal antibody. Furthermore, we showed that the resulting Trx-ELP/anti Trx-mAb complex could be released below the LCST. Our research demonstrates proof-of-principle that "smart," surface-confined biomolecular switches can be built at the nanoscale. Our method of fabricating switchable surfaces is attractive because it is entirely modular and generic, in that it only requires an ELP-modified or patterned surface and a protein that can be appended with an ELP tag. ELP synthesis is easily achieved through genetic engineering techniques. The nanoscale miniaturization of on-chip separation and the presentation and triggered release of the captured proteins made possible by this methodology should be integrable into nanoscale bioanalytical devices that are currently under development.