| AVS 55th International Symposium & Exhibition | |
| Biological, Organic, and Soft Materials Focus Topic | Wednesday Sessions |
| Session BO+AS+BI+NC-WeM |
| Session: | Organized and Structured Organic Interfaces |
| Presenter: | N. Ballav, Universität Heidelberg, Germany |
| Authors: | N. Ballav, Universität Heidelberg, Germany S. Schilp, Universität Heidelberg, Germany T. Winkler, Philipps-Universität Marburg, Germany H. Thomas, Philipps-Universität Marburg, Germany A. Terfort, Philipps-Universität Marburg, Germany M. Zharnikov, Universität Heidelberg, Germany |
| Correspondent: | Click to Email |
The development of novel approaches for the fabrication of nanostructures and, in particular, chemical and biological patterns is an important technological and scientific challenge. One of the perspective methods applies a modification of chemisorbed monomolecular films - self-assembled monolayers (SAMs), which are well-ordered 2D-assembles of long-chain molecules attached to a suitable substrate. A flexible molecular architecture of the SAM constituents allows us to use a wide range of substrates, whereas the molecular size of these constituents makes SAMs an ideal platform for the fabrication of micro- and nanostructures. We present here two new approaches for the fabrication of chemical patterns with aliphatic SAMs as templates. Both approaches rely upon electron beam or X-ray lithography, but require much lower patterning dose as compared to already available methods as, e.g., Chemical Lithography with aromatic templates. The first technique is based on irradiation-promoted exchange reaction (IPER) between the primary SAM template and potential molecular substituent and can utilize a broad variety of commercially available molecules. The key idea of the second method is irradiation-induced activation of amino tail groups of the primary amino-terminated SAM template. Feasibility of both techniques is demonstrated by the fabrication of complex polymer micro- and nanobrushes in a broad height range and, in the case of the IPER approach, by the preparation of micron-scale gradients of protein adhesion.