Bipartite design of a self-fibrillating protein copolymer with nanopatterned peptide display capabilities

Bruning, M. and Kreplak, L. and Leopoldseder, S. and Muller, S. A. and Ringler, P. and Duchesne, L. and Fernig, D. G. and Engel, A. and Ucurum-Fotiadis, Z. and Mayans, O.. (2010) Bipartite design of a self-fibrillating protein copolymer with nanopatterned peptide display capabilities. Nano Letters, Vol. 10, H. 11. pp. 4533-4537.

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Official URL: http://edoc.unibas.ch/dok/A6002458

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The development of biomatrices for technological and biomedical applications employs self-assembled scaffolds built from short peptidic motifs. However, biopolymers composed of protein domains would offer more varied molecular frames to introduce finer and more complex functionalities in bioreactive scaffolds using bottom-up approaches. Yet, the rules governing the three-dimensional organization of protein architectures in nature are complex and poorly understood. As a result, the synthetic fabrication of ordered protein association into polymers poses major challenges to bioengineering. We have now fabricated a self-assembling protein nanofiber with predictable morphologies and amenable to bottom-up customization, where features supporting function and assembly are spatially segregated. The design was inspired by the cross-linking of titin filaments by telethonin in the muscle sarcomere. The resulting fiber is a two-protein system that has nanopatterned peptide display capabilities as shown by the recruitment of functionalized gold nanoparticles at regular intervals of approximately 5 nm, yielding a semiregular linear array over micrometers. This polymer promises the uncomplicated display of biologically active motifs to selectively bind and organize matter in the fine nanoscale. Further, its conceptual design has high potential for controlled plurifunctionalization.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Engel, Andreas H
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Chemical Society
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:13 Oct 2017 07:33
Deposited On:14 Sep 2012 07:15

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