Presentation and recognition of biotin on nanofibers formed by branched peptide amphiphiles.

Nano Lett

Department of Chemistry, Feinberg School of Medicine, Northwestern University, 2220 Campus Drive, Evanston, IL 60208, USA.

Published: February 2005

AI Article Synopsis

  • A new peptide amphiphile system was created to improve the recognition of biotin on self-assembled nanofibers.
  • Branching at a lysine residue allows these peptide amphiphiles to present multiple biotin epitopes on a single molecule, enhancing their effectiveness.
  • Experiments showed that biotinylated branched nanofibers have a better binding affinity with avidin proteins compared to linear peptide structures, confirmed through fluorescence measurements.

Article 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 chromophore-conjugated avidin.

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http://dx.doi.org/10.1021/nl048238zDOI Listing

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