Enzymatic Fabrication of Multifunctional Amyloid-based Protein Assembly

Mitsuki Nakamura; Ryoichi Arai; Noriho Kamiya; Masafumi Sakono

doi:10.1246/cl.230156

Enzymatic Fabrication of Multifunctional Amyloid-based Protein Assembly

Mitsuki Nakamura, Ryoichi Arai, Noriho Kamiya, Masafumi Sakono^*

^*この論文の責任著者

工学科　応用化学コース

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

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We developed a method to orthogonally immobilize multiple functional molecules on amyloid aggregates using different enzymes (sortase A and transglutaminase). Orthogonal binding was performed via the substrate amino acid sequence of each enzyme, and the amount of molecular immobilization could be changed according to the amount of substrate sequence. This method is expected to have applications such as improving the sensitivity of immunoassays and visualization of amyloid elongation reactions.

本文言語	英語
ページ（範囲）	538-541
ページ数	4
ジャーナル	Chemistry Letters
巻	52
号	7
DOI	https://doi.org/10.1246/cl.230156
出版ステータス	出版済み - 2023

ASJC Scopus 主題領域

化学一般

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10.1246/cl.230156

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title = "Enzymatic Fabrication of Multifunctional Amyloid-based Protein Assembly",

abstract = "We developed a method to orthogonally immobilize multiple functional molecules on amyloid aggregates using different enzymes (sortase A and transglutaminase). Orthogonal binding was performed via the substrate amino acid sequence of each enzyme, and the amount of molecular immobilization could be changed according to the amount of substrate sequence. This method is expected to have applications such as improving the sensitivity of immunoassays and visualization of amyloid elongation reactions.",

keywords = "Amyloids, Nanomaterials, Protein assembly",

author = "Mitsuki Nakamura and Ryoichi Arai and Noriho Kamiya and Masafumi Sakono",

note = "Publisher Copyright: {\textcopyright} 2023 The Chemical Society of Japan.",

year = "2023",

doi = "10.1246/cl.230156",

language = "英語",

volume = "52",

pages = "538--541",

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T1 - Enzymatic Fabrication of Multifunctional Amyloid-based Protein Assembly

AU - Nakamura, Mitsuki

AU - Arai, Ryoichi

AU - Kamiya, Noriho

AU - Sakono, Masafumi

PY - 2023

Y1 - 2023

N2 - We developed a method to orthogonally immobilize multiple functional molecules on amyloid aggregates using different enzymes (sortase A and transglutaminase). Orthogonal binding was performed via the substrate amino acid sequence of each enzyme, and the amount of molecular immobilization could be changed according to the amount of substrate sequence. This method is expected to have applications such as improving the sensitivity of immunoassays and visualization of amyloid elongation reactions.

AB - We developed a method to orthogonally immobilize multiple functional molecules on amyloid aggregates using different enzymes (sortase A and transglutaminase). Orthogonal binding was performed via the substrate amino acid sequence of each enzyme, and the amount of molecular immobilization could be changed according to the amount of substrate sequence. This method is expected to have applications such as improving the sensitivity of immunoassays and visualization of amyloid elongation reactions.

KW - Amyloids

KW - Nanomaterials

KW - Protein assembly

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U2 - 10.1246/cl.230156

DO - 10.1246/cl.230156

M3 - 学術論文

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EP - 541

JO - Chemistry Letters

JF - Chemistry Letters

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Enzymatic Fabrication of Multifunctional Amyloid-based Protein Assembly

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