The Amphiphilic Protein HFBII as a Genetically Taggable Molecular Carrier for the Formation of a Self-Organized Functional Protein Layer on a Solid Surface

Hitoshi Asakawa, Shinya Tahara, Momoka Nakamichi, Kenji Takehara, Shinya Ikeno, Markus Linder, Tetsuya Haruyama (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

22 Citations (Scopus)

Abstract

A “drop-stamp method” has been developed for the design and fabrication of molecular interfaces. The amphiphilic protein HFBII, isolated from filamentous fungi, was employed as a genetically taggable molecular carrier for the formation of a structrally ordered layer of functional protein molecules on a solid surface. In this study, the interfacial behavior of maltose-binding protein tagged with HFBII (MBP-HFBII fusion protein) at both the air/water and water/solid interfaces was investigated. A rigid molecular layer of MBP-HFBII fusion protein was successfully formed through the drop-stamp procedure by employing an intermixed system, in which HFBII molecules are intermingled as nanospacers to prevent the intermolecular steric hindrance of the fusion protein. The results show that the drop-stamp method can be utilized in the high-throughput fabrication of structurally ordered molecular interfaces.
Original languageEnglish
Pages (from-to)8841-8844
JournalLangmuir
Volume25
Issue number16
DOIs
Publication statusPublished - 2009
MoE publication typeA1 Journal article-refereed

Fingerprint

solid surfaces
proteins
Proteins
Fusion reactions
fusion
Maltose-Binding Proteins
Maltose
Fabrication
Molecules
Water
fabrication
Fungi
fungi
water
Throughput
molecules
Air
air

Cite this

Asakawa, Hitoshi ; Tahara, Shinya ; Nakamichi, Momoka ; Takehara, Kenji ; Ikeno, Shinya ; Linder, Markus ; Haruyama, Tetsuya. / The Amphiphilic Protein HFBII as a Genetically Taggable Molecular Carrier for the Formation of a Self-Organized Functional Protein Layer on a Solid Surface. In: Langmuir. 2009 ; Vol. 25, No. 16. pp. 8841-8844.
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abstract = "A “drop-stamp method” has been developed for the design and fabrication of molecular interfaces. The amphiphilic protein HFBII, isolated from filamentous fungi, was employed as a genetically taggable molecular carrier for the formation of a structrally ordered layer of functional protein molecules on a solid surface. In this study, the interfacial behavior of maltose-binding protein tagged with HFBII (MBP-HFBII fusion protein) at both the air/water and water/solid interfaces was investigated. A rigid molecular layer of MBP-HFBII fusion protein was successfully formed through the drop-stamp procedure by employing an intermixed system, in which HFBII molecules are intermingled as nanospacers to prevent the intermolecular steric hindrance of the fusion protein. The results show that the drop-stamp method can be utilized in the high-throughput fabrication of structurally ordered molecular interfaces.",
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The Amphiphilic Protein HFBII as a Genetically Taggable Molecular Carrier for the Formation of a Self-Organized Functional Protein Layer on a Solid Surface. / Asakawa, Hitoshi; Tahara, Shinya; Nakamichi, Momoka; Takehara, Kenji; Ikeno, Shinya; Linder, Markus; Haruyama, Tetsuya (Corresponding Author).

In: Langmuir, Vol. 25, No. 16, 2009, p. 8841-8844.

Research output: Contribution to journalArticleScientificpeer-review

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