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Letter

Presentation and Recognition of Biotin on Nanofibers Formed by Branched Peptide Amphiphiles

Supporting Info

Mustafa O. Guler,^† Stephen Soukasene,^‡ James F. Hulvat,^‡ and Samuel I. Stupp*^†^‡^§

Department of Chemistry, Department of Materials Science and Engineering, Feinberg School of Medicine, Northwestern University, 2220 Campus Drive, Evanston, Illinois 60208

Nano Lett., 2005, 5 (2), pp 249–252

DOI: 10.1021/nl048238z

Publication Date (Web): December 29, 2004

†

Department of Chemistry.

‡

Department of Materials Science and Engineering.

Corresponding author. E-mail: s-stupp@northwestern.edu.

Feinberg School of Medicine.

Abstract

A branched peptide amphiphile system was designed for enhanced recognition of biotin on nanofibers formed by self-assembly of these molecules. Branching at a lysine residue was used to design peptide amphiphiles that are capable of presenting more than one epitope per molecule. We found that biotinylated branched structures form nanofibers that enhance recognition by the avidin protein receptor relative to similar nanostructures formed by linear peptide analogues. Biotin−avidin binding to the supramolecular nanofibers was characterized by measurement of fluorescence from nanofibers incubated with chropmophore-conjugated avidin.

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Published In Issue February 09, 2005
Received October 25, 2004
Revised Manuscript Received December 10, 2004

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Letter

Presentation and Recognition of Biotin on Nanofibers Formed by Branched Peptide Amphiphiles

Abstract

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SciFinder Links

History

Recommend & Share

Related Content

Presentation of RGDS Epitopes on Self-Assembled Nanofibers of Branched Peptide Amphiphiles

Heparin Binding Nanostructures to Promote Growth of Blood Vessels

Self-Assembly of Giant Peptide Nanobelts

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