Biocatalytically triggered co-assembly of two-component core/shell nanofibers

Small. 2014 Mar 12;10(5):973-9. doi: 10.1002/smll.201301668. Epub 2013 Sep 11.

Abstract

For the development of applications and novel uses for peptide nanostructures, robust routes for their surface functionalization, that ideally do not interfere with their self-assembly properties, are required. Many existing methods rely on covalent functionalization, where building blocks are appended with functional groups, either pre- or post-assembly. A facile supramolecular approach is demonstrated for the formation of functionalized nanofibers by combining the advantages of biocatalytic self-assembly and surfactant/gelator co-assembly. This is achieved by enzymatically triggered reconfiguration of free flowing micellar aggregates of pre-gelators and functional surfactants to form nanofibers that incorporate and display the surfactants' functionality at the surface. Furthermore, by varying enzyme concentration, the gel stiffness and supramolecular organization of building blocks can be varied.

Keywords: biocatalysis; co-assembly; peptides; surface functionality; transformation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaline Phosphatase / metabolism
  • Biocatalysis*
  • Chromatography, High Pressure Liquid
  • Nanofibers / chemistry*
  • Nanofibers / ultrastructure
  • Oligopeptides / chemistry
  • Spectrometry, Fluorescence
  • Static Electricity
  • Surface-Active Agents / chemistry

Substances

  • Oligopeptides
  • Surface-Active Agents
  • arginyl-glycyl-aspartic acid
  • Alkaline Phosphatase