共 31 条
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
来源:
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.
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页码:538 / 543
页数:6
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