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Bioorthogonal dual functionalization of self-assembling peptide fibers

Paper ID Volume ID Publish Year Pages File Format Full-Text
8315 586 2011 9 PDF Available
Bioorthogonal dual functionalization of self-assembling peptide fibers

The ability to modify peptide- and protein-based biomaterials selectively under mild conditions and in aqueous buffers is essential to the development of certain areas of bionanotechnology, tissue engineering and synthetic biology. Here we show that Self-Assembling peptide Fibers (SAFs) can incorporate multiple modified peptides non-covalently, stoichiometrically and without disrupting their structure or stability. The modified peptides contain groups suitable for post-assembly click reactions in water, namely azides and alkenes. Labeling of these groups is achieved using the orthogonal Cu(I)-catalyzed azide-alkyne and photoinitiated thiol-ene reactions, respectively. Functionalization is demonstrated through the conjugation of biotin followed by streptavidin-nanogold particles, or rhodamine, and visualized by electron and light microscopy, respectively. This has been shown for fibers harboring either or both of the modified peptides. Furthermore, the amounts of each modified peptide in the fibers can be varied with concomitant changes in decoration. This approach allows the design and assembly of fibers with multiple functional components, paving the way for the development of multi-component functionalized systems.

Bioconjugation; Self-assembly; Coiled coil; Fibrous materials; Functionalization
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Bioorthogonal dual functionalization of self-assembling peptide fibers
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 32, Issue 15, May 2011, Pages 3712–3720
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Physical Sciences and Engineering Chemical Engineering Bioengineering