Abstract
We report that the addition of amino acids to the amyloid peptide dramatically affected the structure and the rate of formation of amyloid fibrils. The attachment of three lysines to Aβ(10-35) gave the formation of remarkably long fibrils, while three glutamates resulted in a faster formation rate of the fibrils.
Keywords: Aβ, amyloid, atomic force microscopy, bionanomaterial, fibril formation, self-assembly
Protein & Peptide Letters
Title: Drastic Effects on Fibril Formation of Amyloid-β Peptides by the Addition of Amino Acid Residue Units to the Termini
Volume: 17 Issue: 4
Author(s): Yuya Asanomi, Yumiko Kobayashi, Hiroki Sakai, Takuya Masuda, Xinjiang Chen, Yoshiro Chuman, Kohei Uosaki and Kazuyasu Sakaguchi
Affiliation:
Keywords: Aβ, amyloid, atomic force microscopy, bionanomaterial, fibril formation, self-assembly
Abstract: We report that the addition of amino acids to the amyloid peptide dramatically affected the structure and the rate of formation of amyloid fibrils. The attachment of three lysines to Aβ(10-35) gave the formation of remarkably long fibrils, while three glutamates resulted in a faster formation rate of the fibrils.
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Cite this article as:
Asanomi Yuya, Kobayashi Yumiko, Sakai Hiroki, Masuda Takuya, Chen Xinjiang, Chuman Yoshiro, Uosaki Kohei and Sakaguchi Kazuyasu, Drastic Effects on Fibril Formation of Amyloid-β Peptides by the Addition of Amino Acid Residue Units to the Termini, Protein & Peptide Letters 2010; 17 (4) . https://dx.doi.org/10.2174/092986610790963618
DOI https://dx.doi.org/10.2174/092986610790963618 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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