The Assembly of Individual Chaplin Peptides from Streptomyces coelicolor into Functional Amyloid Fibrils
Elizabeth B Sawyer, Dennis Claessen, Maria Haas, Bhavna Hurgobin, Sally L Gras
PLOS ONE | PUBLIC LIBRARY SCIENCE | Published : 2011
The self-association of proteins into amyloid fibrils offers an alternative to the natively folded state of many polypeptides. Although commonly associated with disease, amyloid fibrils represent the natural functional state of some proteins, such as the chaplins from the soil-dwelling bacterium Streptomyces coelicolor, which coat the aerial mycelium and spores rendering them hydrophobic. We have undertaken a biophysical characterisation of the five short chaplin peptides ChpD-H to probe the mechanism by which these peptides self-assemble in solution to form fibrils. Each of the five chaplin peptides produced synthetically or isolated from the cell wall is individually surface-active and cap..View full abstract
Awarded by Marie Curie Reintegration Grant
EBS was supported by an Endeavour Research Award (Austraining International). DC was supported by a Marie Curie Reintegration Grant (FP7-PEOPLE-ERG-230944). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.