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ACS Nano. 2017 Jul 25;11(7):6764-6772. doi: 10.1021/acsnano.7b01370. Epub 2017 Jun 20.

Salt Triggers the Simple Coacervation of an Underwater Adhesive When Cations Meet Aromatic π Electrons in Seawater.

Author information

1
Department of Chemical and Materials Engineering, University of Alberta , Edmonton, AB T6G 2 V4, Canada.
2
Asia Pacific Center for Theoretical Physics , Pohang 37673, Republic of Korea.
3
Department of Chemistry, Kangwon National University , Chunchon 200-701, Republic of Korea.

Abstract

Adhesive systems in many marine organisms are postulated to form complex coacervates (liquid-liquid phase separation) through a process involving oppositely charged polyelectrolytes. Despite this ubiquitous speculation, most well-characterized mussel adhesive proteins are cationic and polyphenolic, and the pursuit of the negatively charged proteins required for bulk complex coacervation formation internally remains elusive. In this study, we provide a clue for unraveling this paradox by showing the bulky fluid/fluid separation of a single cationic recombinant mussel foot protein, rmfp-1, with no additional anionic proteins or artificial molecules, that is triggered by a strong cation-π interaction in natural seawater conditions. With the similar condition of salt concentration at seawater level (>0.7 M), the electrostatic repulsion between positively charged residues of mfp-1 is screened significantly, whereas the strong cation-π interaction remains unaffected, which leads to the macroscopic phase separation (i.e., bulky coacervate formation). The single polyelectrolyte coacervate shows interesting mechanical properties including low friction, which facilitates the secretion process of the mussel. Our findings reveal that the cation-π interaction modulated by salt is a key mechanism in the mussel adhesion process, providing new insights into the basic understanding of wet adhesion, self-assembly processes, and biological phenomena that are mediated by strong short-range attractive forces in water.

KEYWORDS:

cation−π interaction; mfp-1; protein droplet; simple coacervation; surface forces apparatus

PMID:
28614666
DOI:
10.1021/acsnano.7b01370

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