Journal article
The pH-dependent assembly of Chaplin E from Streptomyces coelicolor
M Dokouhaki, A Hung, L Day, SL Gras
Journal of Structural Biology | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 2017
Abstract
Chaplin E, is one of five self-assembling peptides secreted by Streptomyces coelicolor that assist aerial growth by lowering the surface tension of water. Although the surface activity of a mixture of chaplin peptides has observed to depend on pH, it is unclear how the solvent environment (i.e. pH) influences the structure, assembly and subsequent functionality of these individual peptides. In this study, the conformation and fibril forming propensity of the Chaplin E peptide was assessed as a function of pH using a combination of experimental measurements and molecular dynamics simulations. At an acidic pH of 3.0, Chaplin E retained a random coil structure, whereas at the isoelectric point ..
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Awarded by ARC Dairy Innovation Hub
Funding Acknowledgements
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 the equipment. Sally Gras is supported by The ARC Dairy Innovation Hub (IH2010005).