Deakin University
Browse
prime-structuredependent-2017.pdf (1.25 MB)

Structure-dependent interfacial properties of chaplin F from streptomyces coelicolor

Download (1.25 MB)
Version 3 2024-06-18, 03:56
Version 2 2024-06-04, 07:38
Version 1 2017-10-10, 09:51
journal contribution
posted on 2024-06-18, 03:56 authored by M Dokouhaki, EL Prime, A Hung, GG Qiao, L Day, SL Gras
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.

History

Journal

Biomolecules

Volume

7

Article number

ARTN 68

Pagination

1 - 15

Location

Switzerland

Open access

  • Yes

ISSN

2218-273X

eISSN

2218-273X

Language

English

Notes

Special Issue Functional Amyloids

Publication classification

C Journal article, C1.1 Refereed article in a scholarly journal

Copyright notice

2017, by the authors

Issue

3

Publisher

MDPI