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Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/198954
- Nanopatterning proteins over large areas for biological applications
- Malmstrom, J.; Agheli, H.; Kingshott, P.; Sutherland, D.
- The recent decade has seen a rapid expansion in the ability to create and study nanometer scale objects and these new methods are being applied to the study of biological systems. The immobilisation of bioactive molecules has long been a goal in biomaterials and tissue engineering research, for use as stimulatory cues or model systems to study biointeractions. The advent of soft lithographic routes and efficient approaches to minimise non-specific protein interactions for example through immobilised polyethylene oxide coatings has lead to microscale pattens of proteins were routinely demonstrated and applied as model systems to study biological systems. While patterns at the micrometer scale of considerable interest and application, the size of and lengthscale at which proteins and other macromolecules are structured in vivo is in most cases at the nanoscale. Patterning biomolecules at the nanometer scale gives a significant potential for studying how biological systems function at the macromolecular length scale or to mimic the structure of biological interfaces with macromolecular resolution. A key requisite for the study of cellular biosystems is the ability to robustly generate large areas of patterns. In this work colloidal lithographic routes utilising electrostatic self assembly to generate dispersed monolayers of colloidal particles as masks for pattern generation have been used to generate nanostructured interfaces. Substrates with nanopatterned surface chemistry have been used as templates for generation of nanopatterns of proteins. Hydrophobically modified gold nanopatches in a silicon oxide background have been used to open up arrays of 100nm nanometer diameter regions within a protein rejecting background (based on PLL-g-PEG) and used to demonstrate nanopatterning of a number of protein systems (Laminin, Osteopontin and Ferritin). Nanostructured interfaces have also been fabricated on QCM-D sensors and used to study insitu protein and antibody binding at nanoscale patches while AFM microscopy of dried samples was used to quantify protein and antibody binding utilising height histograms. A combination of QCM-D, AFM and SPR derived data was used to establish the thickness and density of the adsorbed laminin layers at both nanoscale patches and homogeneous surfaces.
- Publication type
- Conference paper
- Paper presented at the 55th American Vacuum Society (AVS) Annual Symposium and Exhibition, Boston, United States, 19-24 October 2008
- Publication year
- AFM; Atomic force microscopy; Bioactive molecultes; Bioactivity; Biological materials; Biomaterials; Colloidal lithography; Laminin; Lithography; Nanometer scale objects; Polyethylene oxide; Protein interactions; Protein patterns; Tissue engineering
- American Vacuum Society
- Publisher URL
- Copyright © 2008.
- Peer reviewed