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Molecular Recognition of Structures Is Key in the Polymerization of Patterned Barnacle Adhesive Sequences
journal contribution
posted on 2019-04-15, 00:00 authored by Christopher R. So, Elizabeth A. Yates, Luis A. Estrella, Kenan P. Fears, Ashley M. Schenck, Catherine M. Yip, Kathryn J. WahlThe 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 noncharged linear sequences 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
antiparallel β-sheet structure as measured by FTIR. While charged
domains favor an antiparallel structure, BCPs without charged domains
switch fibril assembly to favor simpler parallel β-sheet aggregates.
In addition to activation, charged domains direct nanofibers to grow
into discrete microns long fibrils similar to the natural adhesive,
while segments without such domains only form short branched aggregates.
The assembly of adhesive sequences through recognition of structured
templates outlines a strategy used by barnacles to control physical
mechanisms of underwater adhesive delivery, activation, and curing
based on molecular recognition between proteins.
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core segmentbarnacle cementmarine foulantsform amyloid-like materialspeptideactivationfibril formationadult barnaclessequenceantiparallel structuredomains favorrecognitionfibrillar nanomaterialsMolecular Recognitionantiparallel β- sheet structuredomains switch fibril assemblyFTIRBCPβ- sheet aggregatestemplates outlinesproteinPatterned Barnacle Adhesive SequencesPatterned charge domainslink stretches
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