Self-assembly of fused homo-oligomers to create nanotubes

Idit Buch*, Chung Jung Tsai, Haim J. Wolfson, Ruth Nussinov

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

1 Scopus citations

Abstract

The formation of a nanostructure by self-assembly of a peptide or protein building block depends on the ability of the building block to spontaneously assemble into an ordered structure. We first describe a protocol of fusing homo-oligomer proteins with a given three-dimensional (3D) structure to create new building blocks. According to this protocol, a single monomer A that self-assembles with identical copies to create an oligomer A1 is covalently linked, through a short linker L, to another monomer B that self-assembles with identical copies to create the oligomer Bj . The result is a fused monomer A - L - B, which has the ability to self-assemble into a nanostructure (A - L - B)k . We control the self-assembly process of A - L - B by mapping the fused building block onto a planar sheet and wrapping the sheet around a cylinder with the target's dimensions. Finally, we validate the created nanotubes by an optimization procedure. We provide examples of two nanotubes in atomistic model details. One of these has experimental data. In principal, such a protocol should enable the creation of a wide variety of potentially useful protein-based nanotubes with control over their physical and chemical properties.

Original languageEnglish
Title of host publicationNanostructure Design
Subtitle of host publicationMethods and Protocols
PublisherHumana Press
Pages117-131
Number of pages15
ISBN (Print)9781934115350
DOIs
StatePublished - 2008

Publication series

NameMethods in Molecular Biology
Volume474
ISSN (Print)1064-3745

Funding

FundersFunder number
National Cancer InstituteZIABC010442

    Keywords

    • Building block (BB)
    • Homo-oligomers
    • Nanotube
    • Oligomerization domain
    • Self-assembly
    • Symmetry
    • Unit-cell

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