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Simple peptide coacervates adapted for rapid pressure-sensitive wet adhesion.


ABSTRACT: We report here that a dense liquid formed by spontaneous condensation, also known as simple coacervation, of a single mussel foot protein-3S-mimicking peptide exhibits properties critical for underwater adhesion. A structurally homogeneous coacervate is deposited on underwater surfaces as micrometer-thick layers, and, after compression, displays orders of magnitude higher underwater adhesion at 2 N m-1 than that reported from thin films of the most adhesive mussel-foot-derived peptides or their synthetic mimics. The increase in adhesion efficiency does not require nor rely on post-deposition curing or chemical processing, but rather represents an intrinsic physical property of the single-component coacervate. Its wet adhesive and rheological properties correlate with significant dehydration, tight peptide packing and restriction in peptide mobility. We suggest that such dense coacervate liquids represent an essential adaptation for the initial priming stages of mussel adhesive deposition, and provide a hitherto untapped design principle for synthetic underwater adhesives.

SUBMITTER: Kaminker I 

PROVIDER: S-EPMC5744669 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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Simple peptide coacervates adapted for rapid pressure-sensitive wet adhesion.

Kaminker Ilia I   Wei Wei W   Schrader Alex M AM   Talmon Yeshayahu Y   Valentine Megan T MT   Israelachvili Jacob N JN   Waite J Herbert JH   Han Songi S  

Soft matter 20171201 48


We report here that a dense liquid formed by spontaneous condensation, also known as simple coacervation, of a single mussel foot protein-3S-mimicking peptide exhibits properties critical for underwater adhesion. A structurally homogeneous coacervate is deposited on underwater surfaces as micrometer-thick layers, and, after compression, displays orders of magnitude higher underwater adhesion at 2 N m<sup>-1</sup> than that reported from thin films of the most adhesive mussel-foot-derived peptide  ...[more]

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