Toward Artificial Mussel-Glue Proteins: Differentiating Sequence Modules for Adhesion and Switchable Cohesion.
adhesion
cohesion control
enzyme-induced polymerization
mussel glue
synthetic proteins
Journal
Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543
Informations de publication
Date de publication:
12 10 2020
12 10 2020
Historique:
received:
16
06
2020
pubmed:
1
7
2020
medline:
1
7
2020
entrez:
30
6
2020
Statut:
ppublish
Résumé
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
Identifiants
pubmed: 32596967
doi: 10.1002/anie.202008515
pmc: PMC7590116
doi:
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
18495-18499Subventions
Organisme : Austrian Science Fund FWF
ID : P 32326
Pays : Austria
Informations de copyright
© 2020 The Authors. Published by Wiley-VCH GmbH.
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