Directed three-dimensional patterning of self-assembled peptide fibrils

被引:80
作者
Dinca, Valentina [1 ]
Kasotakis, Emmanouil [2 ]
Catherine, Julien [1 ]
Mourka, Areti [1 ,3 ]
Ranella, Anthi [1 ]
Ovsianikov, Aleksandr [4 ]
Chichkov, Boris N. [1 ,4 ]
Farsari, Maria [1 ]
Mitraki, Anna [1 ,2 ]
Fotakis, Costas [1 ,3 ]
机构
[1] Fdn Res & Technol Hellas, Inst Elect Struct & Laser, GR-71110 Iraklion, Greece
[2] Univ Crete, Dept Mat Sci & Technol, Iraklion, Greece
[3] Univ Crete, Dept Phys, Iraklion, Greece
[4] Laser Zentrum Hannover, D-30419 Hannover, Germany
关键词
D O I
10.1021/nl072798r
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:538 / 543
页数:6
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