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

Research output: Contribution to journalArticlepeer-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 languageAmerican English
Pages (from-to)1575-1579
Number of pages5
JournalNano Letters
Volume7
Issue number6
DOIs
StatePublished - Jun 2007

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