Creating ultrathin nanoscopic collagen matrices for biological and biotechnological applications.
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 (approximately 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.
Cisneros
David A
DA
BIOTEC, University of Technology Dresden, Tatzberg 47-51, 01307 Dresden, Germany.
Friedrichs
Jens
J
Taubenberger
Anna
A
Franz
Clemens M
CM
Muller
Daniel J
DJ
D000818:Animals; D001696:Biomechanical Phenomena; D001709:Biotechnology / Q000295:instrumentation*; D002021:Buffers; D002448:Cell Adhesion; D002465:Cell Movement; D016764:Cell Polarity; D004573:Electrolytes; D024022:Fibrillar Collagens / Q000737:chemistry* / Q000648:ultrastructure*; D006863:Hydrogen-Ion Concentration; D018625:Microscopy, Atomic Force; D049329:Nanostructures / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D051381:Rats
D002021:Buffers; D004573:Electrolytes; D024022:Fibrillar Collagens