Investigation of self-assembling proline- and glycine-rich recombinant proteins and peptides inspired by proteins from a symbiotic fungus using atomic force microscopy and circular dichroism spectroscopy

Creasey, Rhiannon G., Voelcker, Nicolas H. and Schultz, Carolyn J. (2012) Investigation of self-assembling proline- and glycine-rich recombinant proteins and peptides inspired by proteins from a symbiotic fungus using atomic force microscopy and circular dichroism spectroscopy. Biochimica et Biophysica Acta - Proteins and Proteomics, 1824 5: 711-722. doi:10.1016/j.bbapap.2012.02.009


Author Creasey, Rhiannon G.
Voelcker, Nicolas H.
Schultz, Carolyn J.
Title Investigation of self-assembling proline- and glycine-rich recombinant proteins and peptides inspired by proteins from a symbiotic fungus using atomic force microscopy and circular dichroism spectroscopy
Journal name Biochimica et Biophysica Acta - Proteins and Proteomics   Check publisher's open access policy
ISSN 1570-9639
Publication date 2012-01-01
Year available 2012
Sub-type Article (original research)
DOI 10.1016/j.bbapap.2012.02.009
Open Access Status Not yet assessed
Volume 1824
Issue 5
Start page 711
End page 722
Total pages 12
Place of publication Amsterdam, The Netherlands
Publisher Elsevier
Language eng
Abstract Fiber-forming proteins and peptides are being scrutinized as a promising source of building blocks for new nanomaterials. Arabinogalactan-like (AGL) proteins expressed at the symbiotic interface between plant roots and arbuscular mycorrhizal fungi have novel sequences, hypothesized to form polyproline II (PPII) helix structures. The functional nature of these proteins is unknown but they may form structures for the establishment and maintenance of fungal hyphae. Here we show that recombinant AGL1 (rAGL1) and recombinant AGL3 (rAGL3) are extended proteins based upon secondary structural characteristics determined by electronic circular dichroism (CD) spectroscopy and can self-assemble into fibers and microtubes as observed by atomic force microscopy (AFM) and scanning electron microscopy (SEM). CD spectroscopy results of synthetic peptides based on repeat regions in AGL1, AGL2 and AGL3 suggest that the synthetic peptides contain significant amounts of extended PPII helices and that these structures are influenced by ionic strength and, at least in one case, by concentration. Point mutations of a single residue of the repeat region of AGL3 resulted in altered secondary structures. Self-assembly of these repeats was observed by means of AFM and optical microscopy. Peptide (APADGK)6 forms structures with similar morphology to rAGL1 suggesting that these repeats are crucial for the morphology of rAGL1 fibers. These novel self-assembling sequences may find applications as precursors for bioinspired nanomaterials.
Keyword Amphipathic peptide
Arabinogalactan-like protein
Atomic force microscopy
Circular dichroism spectroscopy
Mycorrhizal symbiosis
Self assembly
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemical Engineering Publications
 
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Created: Tue, 15 Sep 2015, 20:26:16 EST by Noni Creasey on behalf of School of Chemical Engineering