Journal article
Structure-dependent interfacial properties of chaplin F from streptomyces coelicolor
M Dokouhaki, EL Prime, A Hung, GG Qiao, L Day, SL Gras
Biomolecules | MDPI | Published : 2017
DOI: 10.3390/biom7030068
Abstract
Chaplin F (Chp F) is a secreted surface-active peptide involved in the aerial growth of Streptomyces. While Chp E demonstrates a pH-responsive surface activity, the relationship between Chp F structure, function and the effect of solution pH is unknown. Chp F peptides were found to self-assemble into amyloid fibrils at acidic pH (3.0 or the isoelectric point (pI) of 4.2), with ~99% of peptides converted into insoluble fibrils. In contrast, Chp F formed short assemblies containing a mixture of random coil and β-sheet structure at a basic pH of 10.0, where only 40% of the peptides converted to fibrils. The cysteine residues in Chp F did not appear to play a role in fibril assembly. The interfa..
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Funding Acknowledgements
The authors wish to acknowledge the Electron Microscopy Unit of The University of Melbourne, for assistance with electron microscopy, in particular Simon Crawford. The authors would like to acknowledge the Australian Government for providing the Australian Postgraduate Award (APA) and International Postgraduate Research Scholarship (IPRS). The authors also thank the Particulate Fluids Processing Centre (PFPC) and the Bio21 Institute for access to the equipment. Sally L. Gras is supported by The ARC Dairy Innovation Hub (IH2010005). Emma L. Prime is supported by the ARC Research Hub for Future Fibres (IH140100018). Andrew Hung acknowledges the assistance of the National Computational Infrastructure (NCI).