{"language":[{"iso":"eng"}],"date_updated":"2022-01-06T06:59:56Z","type":"journal_article","publication":"Langmuir","article_type":"original","author":[{"full_name":"Rüdiger, Arne A.","last_name":"Rüdiger","first_name":"Arne A."},{"first_name":"Katharina","last_name":"Brassat","id":"11305","full_name":"Brassat, Katharina"},{"first_name":"Jörg","last_name":"Lindner","id":"20797","full_name":"Lindner, Jörg"},{"first_name":"Wolfgang","last_name":"Bremser","full_name":"Bremser, Wolfgang"},{"first_name":"Oliver I.","full_name":"Strube, Oliver I.","last_name":"Strube"}],"publisher":"American Chemical Society (ACS)","year":"2018","status":"public","intvolume":"        34","user_id":"55706","citation":{"ieee":"A. A. Rüdiger, K. Brassat, J. Lindner, W. Bremser, and O. I. Strube, “Easily Accessible Protein Nanostructures via Enzyme Mediated Addressing,” <i>Langmuir</i>, vol. 34, no. 14, pp. 4264–4270, 2018.","mla":"Rüdiger, Arne A., et al. “Easily Accessible Protein Nanostructures via Enzyme Mediated Addressing.” <i>Langmuir</i>, vol. 34, no. 14, American Chemical Society (ACS), 2018, pp. 4264–70, doi:<a href=\"https://doi.org/10.1021/acs.langmuir.7b04089\">10.1021/acs.langmuir.7b04089</a>.","bibtex":"@article{Rüdiger_Brassat_Lindner_Bremser_Strube_2018, title={Easily Accessible Protein Nanostructures via Enzyme Mediated Addressing}, volume={34}, DOI={<a href=\"https://doi.org/10.1021/acs.langmuir.7b04089\">10.1021/acs.langmuir.7b04089</a>}, number={14}, journal={Langmuir}, publisher={American Chemical Society (ACS)}, author={Rüdiger, Arne A. and Brassat, Katharina and Lindner, Jörg and Bremser, Wolfgang and Strube, Oliver I.}, year={2018}, pages={4264–4270} }","ama":"Rüdiger AA, Brassat K, Lindner J, Bremser W, Strube OI. Easily Accessible Protein Nanostructures via Enzyme Mediated Addressing. <i>Langmuir</i>. 2018;34(14):4264-4270. doi:<a href=\"https://doi.org/10.1021/acs.langmuir.7b04089\">10.1021/acs.langmuir.7b04089</a>","apa":"Rüdiger, A. A., Brassat, K., Lindner, J., Bremser, W., &#38; Strube, O. I. (2018). Easily Accessible Protein Nanostructures via Enzyme Mediated Addressing. <i>Langmuir</i>, <i>34</i>(14), 4264–4270. <a href=\"https://doi.org/10.1021/acs.langmuir.7b04089\">https://doi.org/10.1021/acs.langmuir.7b04089</a>","short":"A.A. Rüdiger, K. Brassat, J. Lindner, W. Bremser, O.I. Strube, Langmuir 34 (2018) 4264–4270.","chicago":"Rüdiger, Arne A., Katharina Brassat, Jörg Lindner, Wolfgang Bremser, and Oliver I. Strube. “Easily Accessible Protein Nanostructures via Enzyme Mediated Addressing.” <i>Langmuir</i> 34, no. 14 (2018): 4264–70. <a href=\"https://doi.org/10.1021/acs.langmuir.7b04089\">https://doi.org/10.1021/acs.langmuir.7b04089</a>."},"volume":34,"title":"Easily Accessible Protein Nanostructures via Enzyme Mediated Addressing","_id":"3925","publication_identifier":{"issn":["0743-7463","1520-5827"]},"department":[{"_id":"286"},{"_id":"2"},{"_id":"15"}],"publication_status":"published","issue":"14","ddc":["530"],"file":[{"file_id":"3926","file_name":"Easily accessible protein nanostructures via enzyme mediated addressing_2018.pdf","success":1,"date_created":"2018-08-16T13:05:39Z","date_updated":"2018-08-16T13:05:39Z","creator":"hclaudia","file_size":4951412,"access_level":"closed","content_type":"application/pdf","relation":"main_file"}],"page":"4264-4270","doi":"10.1021/acs.langmuir.7b04089","abstract":[{"text":"Site-specific formation of nanoscaled protein structures is a challenging task. Most known structuring\r\nmethods are either complex and hardly upscalable or do not apply to biological matter at all. The presented combination of enzyme mediated autodeposition and nanosphere lithography provides an easy-to-apply approach for the buildup of protein nanostructures over a large scale. The key factor is the tethering of enzyme to the support in designated areas. Those areas are provided via prepatterning of enzymatically active antidots with variable diameters. Enzymatically triggered protein addressing occurs exclusively at the intended areas and continues until the entire active area is coated. After this, the reaction self-terminates. The major advantage of the presented method lies in its easy applicability and upscalability. Large area structuring of entire support surfaces with features on the nanometer scale is performed efficiently and without the necessity of harsh conditions. These are valuable premises for large-scale applications with potentials in biosensor technology, nanoelectronics, and life sciences.","lang":"eng"}],"has_accepted_license":"1","date_created":"2018-08-16T13:04:54Z","file_date_updated":"2018-08-16T13:05:39Z"}