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Toward Artificial Mussel‐Glue Proteins: Differentiating Sequence Modules for Adhesion and Switchable Cohesion
Author(s) -
Arias Sandra,
Amini Shahrouz,
Horsch Justus,
Pretzler Matthias,
Rompel Annette,
Melnyk Inga,
Sychev Dmitrii,
Fery Andreas,
Börner Hans G.
Publication year - 2020
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202008515
Subject(s) - glue , polymerization , adhesive , cohesion (chemistry) , adsorption , materials science , coating , nanoindentation , chemical engineering , chemistry , polymer chemistry , biophysics , nanotechnology , composite material , polymer , organic chemistry , layer (electronics) , biology , engineering
Artificial mussel‐glue proteins with pH‐triggered cohesion control were synthesized by extending the tyrosinase activated polymerization of peptides to sequences with specific modules for cohesion control. The high propensity of these sequence sections to adopt β‐sheets is suppressed by switch defects. This allows enzymatic activation and polymerization to proceed undisturbed. The β‐sheet formation is regained after polymerization by changing the pH from 5.5 to 6.8, thereby triggering O→N acyl transfer rearrangements that activate the cohesion mechanism. The resulting artificial mussel glue proteins exhibit rapid adsorption on alumina surfaces. The coatings resist harsh hypersaline conditions, and reach remarkable adhesive energies of 2.64 mJ m −2 on silica at pH 6.8. In in situ switch experiments, the minor pH change increases the adhesive properties of a coating by 300 % and nanoindentation confirms the cohesion mechanism to improve bulk stiffness by around 200 %.