Directed three-dimensional patterning of self-assembled peptide fibrils

Nano Lett. 2008 Feb;8(2):538-43. doi: 10.1021/nl072798r. Epub 2007 Dec 23.

Abstract

Molecular self-assembly is emerging as a viable "bottom-up" approach for fabricating nanostructures. Self-assembled biomolecular structures are particularly attractive, due to their versatile chemistry, molecular recognition properties, and biocompatibility. Among them, amyloid protein and peptide fibrils are self-assembled nanostructures with unique physical and chemical stability, formed from quite simple building blocks; their ability to work as a template for the fabrication of low resistance, conducting nanowires has already been demonstrated. The precise positioning of peptide-based nanostructures is an essential part of their use in technological applications, and their controlled assembly, positioning, and integration into microsystems is a problem of considerable current interest. To date, their positioning has been limited to their placement on flat surfaces or to the fabrication of peptide arrays. Here, we propose a new method for the precise, three-dimensional patterning of amyloid fibrils. The technique, which combines femtosecond laser technology and biotin-avidin mediated assembly on a polymeric matrix, can be applied in a wide variety of fields, from molecular electronics to tissue engineering.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Binding Sites
  • Crystallization / methods*
  • Macromolecular Substances / chemistry
  • Materials Testing
  • Molecular Conformation
  • Nanostructures / chemistry*
  • Nanostructures / ultrastructure*
  • Nanotechnology / methods*
  • Particle Size
  • Peptides / chemistry*
  • Protein Binding
  • Surface Properties

Substances

  • Macromolecular Substances
  • Peptides