Molecular Recognition of Structures Is Key in the Polymerization of Patterned Barnacle Adhesive Sequences

The permanent adhesive produced by adult barnacles is held together by tightly folded proteins that form amyloid-like materials distinct among marine foulants. In this work, we link stretches of alternating charged and non-charged linear sequence from a family of adhesive proteins to their role in forming fibrillar nanomaterials. Using recombinant proteins and short barnacle cement derived peptides (BCPs), we find a central sequence with charged motifs of the pattern [Gly/Ser/Val/Thr/Ala -X], where X are charged amino acids, to exert specific control over timing, structure and morphology of fibril formation. While most BCPs remain dormant, the core segment demonstrates rapid polymerization as well as an ability to template other peptides with no propensity for self-assembly. Patterned charge domains assemble dormant peptides through a specific anti-parallel beta sheet structure as measured by FTIR. While charged domains favor an anti-parallel structure, BCPs without charged domains switch fibril assembly ...