Structure-dependent interfacial properties of Chaplin F from Streptomyces coelicolor

Dokouhaki, Mina, Prime, Emma, Hung, Andrew, Qiao, Greg G., Day, Li and Gras, Sally L. 2017, Structure-dependent interfacial properties of Chaplin F from Streptomyces coelicolor, Biomolecules, vol. 7, no. 3, pp. 1-15, doi: 10.3390/biom7030068.

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Title Structure-dependent interfacial properties of Chaplin F from Streptomyces coelicolor
Formatted title Structure-dependent interfacial properties of Chaplin F from Streptomyces coelicolor
Author(s) Dokouhaki, Mina
Prime, EmmaORCID iD for Prime, Emma orcid.org/0000-0002-1410-6717
Hung, Andrew
Qiao, Greg G.
Day, Li
Gras, Sally L.
Journal name Biomolecules
Volume number 7
Issue number 3
Start page 1
End page 15
Total pages 15
Publisher MDPI
Place of publication Basel, Switzerland
Publication date 2017-09
ISSN 2218-273X
Keyword(s) Brewster angle microscopy
atomic force microscopy
circular dichroism
pressure/area isotherms
self-assembly
Amyloid
Bacterial Proteins
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Protein Structure, Secondary
Streptomyces coelicolor
Summary 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 interfacial properties of Chp F at the air/water interface were altered by the structures adopted at different pH, with Chp F molecules forming a higher surface-active film at pH 10.0 with a lower area per molecule compared to Chp F fibrils at pH 3.0. These data show that the pH responsiveness of Chp F surface activity is the reverse of that observed for Chp E, which could prove useful in potential applications where surface activity is desired over a wide range of solution pH.
Notes Special Issue Functional Amyloids
Language eng
DOI 10.3390/biom7030068
Field of Research 030403 Characterisation of Biological Macromolecules
030603 Colloid and Surface Chemistry
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Grant ID IH140100018
Copyright notice ©2017, by the authors
Persistent URL http://hdl.handle.net/10536/DRO/DU:30103162

Document type: Journal Article
Collection: Institute for Frontier Materials
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