Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues

A novel strategy to generate adhesive protein analogues by enzyme‐induced polymerization of peptides is reported. Peptide polymerization relies on tyrosinase oxidation of tyrosine residues to Dopaquinones, which rapidly form cysteinyldopa‐moieties with free thiols from cysteine residues, thereby lin...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2018-11, Vol.57 (48), p.15728-15732
Main Authors: Horsch, Justus, Wilke, Patrick, Pretzler, Matthias, Seuss, Maximilian, Melnyk, Inga, Remmler, Dario, Fery, Andreas, Rompel, Annette, Börner, Hans G.
Format: Article
Language:English
Subjects:
Adhesion
Adhesive strength
Adhesives
Adhesives - chemistry
Adhesives - metabolism
Adsorption
Animals
Benzoquinones - chemistry
Benzoquinones - metabolism
Biomimetic Materials - chemistry
Biomimetic Materials - metabolism
Bivalvia - chemistry
Bivalvia - metabolism
Communication
Communications
Cysteine - chemistry
Cysteine - metabolism
Dihydroxyphenylalanine - analogs & derivatives
Dihydroxyphenylalanine - chemistry
Dihydroxyphenylalanine - metabolism
enzyme-induced polymerization
Glues
Gluing
Interfaces
Molecular Structure
Mollusks
Monophenol Monooxygenase - chemistry
Monophenol Monooxygenase - metabolism
mussel glue
Mussels
Oxidation
Peptides
Polymerization
Polymers
Proteins
Proteins - chemistry
Proteins - metabolism
Residues
Surface Properties
synthetic protein mimics
Thiols
Tyrosinase
tyrosinase activation
Tyrosine
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Summary:A novel strategy to generate adhesive protein analogues by enzyme‐induced polymerization of peptides is reported. Peptide polymerization relies on tyrosinase oxidation of tyrosine residues to Dopaquinones, which rapidly form cysteinyldopa‐moieties with free thiols from cysteine residues, thereby linking unimers and generating adhesive polymers. The resulting artificial protein analogues show strong adsorption to different surfaces, even resisting hypersaline conditions. Remarkable adhesion energies of up to 10.9 mJ m−2 are found in single adhesion events and average values are superior to those reported for mussel foot proteins that constitute the gluing interfaces. Mussel glue protein mimics: Adhesive mussel‐inspired protein analogues were prepared by an enzyme‐induced polymerization of oligopeptides. The polymers are generated by the formation of cysteinyldopa linkages that contribute to cohesion and adhesion of the protein analogues. Aspects of adhesion properties of mussel foot proteins were mimicked without the need to extract and purify or express native proteins.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201809587