Bioorthogonal dual functionalization of self-assembling peptide fibers

ZN Mahmoud, SB Gunnoo, A R Thomson, JM Fletcher, DN Woolfson

Research output: Contribution to journalArticle (Academic Journal)peer-review

55 Citations (Scopus)


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.
Translated title of the contributionBioorthogonal dual functionalization of self-assembling peptide fibers
Original languageEnglish
Pages (from-to)3712 - 3720
Number of pages9
Volume32 (15)
Publication statusPublished - May 2011

Structured keywords

  • Bristol BioDesign Institute




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