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Biomolecules 2017, 7(3), 68; doi:10.3390/biom7030068

Structure-Dependent Interfacial Properties of Chaplin F from Streptomyces coelicolor

1
Department of Chemical Engineering and The Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC 3010, Australia
2
Institute for Frontier Materials, Deakin University, Geelong, VIC 3216, Australia
3
Polymer Science Group, Department of Chemical Engineering, The University of Melbourne, Parkville, VIC 3010, Australia
4
School of Science, RMIT University, Melbourne, VIC 3001, Australia
5
AgResearch Ltd, Grasslands Research Centre, Tennent Drive, Palmerston North 4442, New Zealand
6
The ARC Dairy Innovation Hub, The University of Melbourne, Parkville, VIC 3010, Australia
*
Author to whom correspondence should be addressed.
Academic Editors: Matthew Chapman and Daniel Otzen
Received: 27 July 2017 / Revised: 8 September 2017 / Accepted: 12 September 2017 / Published: 19 September 2017
(This article belongs to the Special Issue Functional Amyloids)
View Full-Text   |   Download PDF [11347 KB, uploaded 20 September 2017]   |  

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 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. View Full-Text
Keywords: self-assembly; pressure/area isotherms; circular dichroism; atomic force microscopy; Brewster angle microscopy self-assembly; pressure/area isotherms; circular dichroism; atomic force microscopy; Brewster angle microscopy
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Dokouhaki, M.; Prime, E.L.; Hung, A.; Qiao, G.G.; Day, L.; Gras, S.L. Structure-Dependent Interfacial Properties of Chaplin F from Streptomyces coelicolor. Biomolecules 2017, 7, 68.

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