Hierarchical and helical self-assembly of ADP-ribosyl cyclase into large-scale protein microtubes

Qun Liu, Irina A. Kriksunov, Zhongwu Wang, Richard M Graeff, Hon Cheung Lee, Quan Hao

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

Abstract

Proteins are macromolecules with characteristic structures and biological functions. It is extremely challenging to obtain protein microtube structures through self-assembly as proteins are very complex and flexible. Here we present a strategy showing how a specific protein, ADP-ribosyl cyclase, helically self-assembles from monomers into hexagonal nanochains and further to highly ordered crystalline microtubes. The structures of protein nanochains and consequently self-assembled superlattice were determined by X-ray crystallography at 4.5 Å resolution and imaged by scanning electron microscopy. The protein initially forms into dimers that have a fixed size of 5.6 nm, and then, helically self-assembles into 35.6 nm long hexagonal nanochains. One such nanochain consists of six dimers (12 monomers) that stack in order by a pseudo P61 screw axis. Seven nanochains produce a series of large-scale assemblies, nanorods, forming the building blocks for microrods. A proposed aging process of microrods results in the formation of hollow microstructures. Synthesis and characterization of large scale self-assembled protein microtubes may pave a new pathway, capable of not only understanding the self-assembly dynamics of biological materials, but also directing design and fabrication of multifunctional nanobuilding blocks with particular applications in biomedical engineering.

Original languageEnglish (US)
Pages (from-to)14682-14686
Number of pages5
JournalJournal of Physical Chemistry B
Volume112
Issue number47
DOIs
StatePublished - Nov 27 2008

Fingerprint Dive into the research topics of 'Hierarchical and helical self-assembly of ADP-ribosyl cyclase into large-scale protein microtubes'. Together they form a unique fingerprint.

Cite this