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Formation of Functionalized Nanowires by Control of Self‐Assembly Using Multiple Modified Amyloid Peptides
Author(s) -
Sakai Hiroki,
Watanabe Ken,
Asanomi Yuya,
Kobayashi Yumiko,
Chuman Yoshiro,
Shi Lihong,
Masuda Takuya,
Wyttenbach Thomas,
Bowers Michael T.,
Uosaki Kohei,
Sakaguchi Kazuyasu
Publication year - 2013
Publication title -
advanced functional materials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.069
H-Index - 322
eISSN - 1616-3028
pISSN - 1616-301X
DOI - 10.1002/adfm.201300577
Subject(s) - materials science , amyloid fibril , nanowire , self assembly , peptide , fibril , nanotechnology , amyloid (mycology) , residue (chemistry) , biophysics , amyloid β , chemistry , biochemistry , medicine , inorganic chemistry , disease , pathology , biology
Amyloid peptides have great potential as building blocks in the creation of functional nanowires due to their natural ability to self‐assemble into nanofibrillar structures and because they can be easily modified with various functional groups. However, significant modifications of an amyloid peptide generally alter its self‐assembly property, making it difficult to construct functionalized fibrils with a desired structure and function. In this study, a very effective method to overcome this problem is demonstrated by using our structure‐controllable amyloid peptides (SCAPs) terminated with a three‐amino‐acid‐residue cap. The method consists on mixing two or more structurally related amyloid peptides with a fraction of modified SCAPs which co‐assemble into a fibril. This SCAP‐mixing method provides remarkable control over the self‐assembly process both on the small oligomers level and the macroscopic fibrils level. Furthermore, it is shown that the modified peptides imbedded in the resulting fibril can subsequently be functionalized to generate nanowires with the desired properties, highlighting the importance of this SCAP method for nanotechnology applications.