1. Directed three-dimensional patterning of self-assembled peptide fibrils
- Author
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Areti Mourka, Emmanouil Kasotakis, Anthi Ranella, Maria Farsari, Costas Fotakis, Valentina Dinca, Anna Mitraki, Julien Catherine, Boris N. Chichkov, and Aleksandr Ovsianikov
- Subjects
Fabrication ,Nanostructure ,Biocompatibility ,Macromolecular Substances ,Surface Properties ,Nanowire ,Molecular Conformation ,Bioengineering ,Nanotechnology ,Molecular recognition ,Materials Testing ,General Materials Science ,Particle Size ,Binding Sites ,Chemistry ,Mechanical Engineering ,Molecular electronics ,General Chemistry ,Condensed Matter Physics ,Nanostructures ,Template reaction ,Self-assembly ,Adsorption ,Crystallization ,Peptides ,Protein Binding - 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.
- Published
- 2007