The assembly of individual chaplin peptides from Streptomyces coelicolor into functional amyloid fibrils.

ABSTRACT: 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 capable of forming fibrils under a range of solution conditions in vitro. These fibrils contain a highl

SUBMITTER: Sawyer EB 

PROVIDER: S-EPMC3079736 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature