SP1 as a novel scaffold building block for self-assembly nanofabrication of submicron enzymatic structures

Arnon Heyman; Ilan Levy; Arie Altman; Oded Shoseyov

doi:10.1021/nl070450q

SP1 as a novel scaffold building block for self-assembly nanofabrication of submicron enzymatic structures

Arnon Heyman, Ilan Levy, Arie Altman, Oded Shoseyov^*

^*Corresponding author for this work

Institute of Plant Sciences and Genetics in Agriculture

Research output: Contribution to journal › Article › peer-review

36 Scopus citations

Abstract

In this study, SP1, a ring-shaped highly stable homododecamer protein complex was utilized for the self-assembly of multiple domains in a predefined manner. Glucose oxidase (GOx) was fused in-frame to SP1 and expressed in Escherichia coli. Complexes where GOx encircled SP1 dodecamer were observed, and moreover, the enzymatic monomers self-assembled into active multienzyme nanotube particles containing hundreds of GOx molecules per tube. This work demonstrates the value of SP1 as a self-assembly scaffold.

Original language	English
Pages (from-to)	1575-1579
Number of pages	5
Journal	Nano Letters
Volume	7
Issue number	6
DOIs	https://doi.org/10.1021/nl070450q
State	Published - Jun 2007

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10.1021/nl070450q

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SP1 as a novel scaffold building block for self-assembly nanofabrication of submicron enzymatic structures

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