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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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Autores principales: Horsch, Justus, Wilke, Patrick, Pretzler, Matthias, Seuss, Maximilian, Melnyk, Inga, Remmler, Dario, Fery, Andreas, Rompel, Annette, Börner, Hans G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6282983/
https://www.ncbi.nlm.nih.gov/pubmed/30246912
http://dx.doi.org/10.1002/anie.201809587
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author Horsch, Justus
Wilke, Patrick
Pretzler, Matthias
Seuss, Maximilian
Melnyk, Inga
Remmler, Dario
Fery, Andreas
Rompel, Annette
Börner, Hans G.
author_facet Horsch, Justus
Wilke, Patrick
Pretzler, Matthias
Seuss, Maximilian
Melnyk, Inga
Remmler, Dario
Fery, Andreas
Rompel, Annette
Börner, Hans G.
author_sort Horsch, Justus
collection PubMed
description 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.
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spelling pubmed-62829832018-12-14 Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues Horsch, Justus Wilke, Patrick Pretzler, Matthias Seuss, Maximilian Melnyk, Inga Remmler, Dario Fery, Andreas Rompel, Annette Börner, Hans G. Angew Chem Int Ed Engl Communications 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. John Wiley and Sons Inc. 2018-10-31 2018-11-26 /pmc/articles/PMC6282983/ /pubmed/30246912 http://dx.doi.org/10.1002/anie.201809587 Text en © 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Communications
Horsch, Justus
Wilke, Patrick
Pretzler, Matthias
Seuss, Maximilian
Melnyk, Inga
Remmler, Dario
Fery, Andreas
Rompel, Annette
Börner, Hans G.
Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues
title Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues
title_full Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues
title_fullStr Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues
title_full_unstemmed Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues
title_short Polymerizing Like Mussels Do: Toward Synthetic Mussel Foot Proteins and Resistant Glues
title_sort polymerizing like mussels do: toward synthetic mussel foot proteins and resistant glues
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6282983/
https://www.ncbi.nlm.nih.gov/pubmed/30246912
http://dx.doi.org/10.1002/anie.201809587
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