Creating ultrathin nanoscopic collagen matrices for biological and biotechnological applications

Research output: Contribution to journalResearch articleContributedpeer-review


  • David A. Cisneros - , TUD Dresden University of Technology (Author)
  • Jens Friedrichs - , TUD Dresden University of Technology (Author)
  • Anna Taubenberger - , TUD Dresden University of Technology (Author)
  • Clemens M. Franz - , TUD Dresden University of Technology (Author)
  • Daniel J. Muller - , TUD Dresden University of Technology (Author)


The biofunctionalization of materials creates interfaces on which proteins, cells, or tissues can fulfill native or desired tasks. Here we report how to control the assembly of type I collagen into well-defined nanoscopic matrices of different patterns. Collagen fibrils in these ultrathin ≈ 3 nm) matrices maintained their native structure as observed in vivo. This opens up the possibility to create programmable biofunctionalized matrices using collagen-binding proteins or proteins fused with collagen-binding domains. Applied to eukaryotic cells, these nanostructured matrices can direct cellular processes such as adhesion, orientation and migration.


Original languageEnglish
Pages (from-to)956-963
Number of pages8
Issue number6
Publication statusPublished - Jun 2007
Externally publishedYes

External IDs

PubMed 17394282



  • Atomic force microscopy, Biofunctionalization, Biomaterials, Collagen, Self-assembly