Nanostructure Fabrication Based on Engineered α-Synuclein View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2008-12

AUTHORS

Natsuki Kobayashi, Sungwoong Han, Chikashi Nakamura, Koji Sode

ABSTRACT

The utilization of biomaterials such as proteins or peptides has recently been focused on as an attractive way to construct nanomaterials by “bottom-up” strategy. We focus on α-synuclein as a novel scaffold material for functional nanomaterial fabrication. This protein constructs an amyloid-like nanostructure by self-assembly under mild conditions. In this paper, we demonstrate nanomaterial fabrication by utilizing two peptide fragments of the non-amyloid-β component of Alzheimer’s disease amyloid region, which is the key region for α-synuclein fibrillation. One of these peptide fragments contains the sequence corresponding to residues 66–82 of wild-type α-synuclein, while the other contains the same region from the Val70Thr/Val71Thr mutant, whose character is drastically different. In this paper, we confirmed that these two peptides individually formed different rod-like structures. Moreover, these peptides modify the fibril nanostructure of full-length α-synuclein, and these effects depend on the peptide sequences. Therefore, we propose the combination of amyloid-forming protein, and its partial peptide fragments with some mutations have a potential for novel nanomaterial fabrication. More... »

PAGES

50-55

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12030-008-9011-3

DOI

http://dx.doi.org/10.1007/s12030-008-9011-3

DIMENSIONS

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