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Implementing Zn2+ ion and pH-value control into artificial mussel glue proteins by abstracting a His-rich domain from preCollagen

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Amini,  Shahrouz
Shahrouz Amini, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

Arias, S., Amini, S., Krüger, J. M., Bangert, L. D., & Börner, H. G. (2021). Implementing Zn2+ ion and pH-value control into artificial mussel glue proteins by abstracting a His-rich domain from preCollagen. Soft Matter. doi:10.1039/D0SM02118K.


Cite as: http://hdl.handle.net/21.11116/0000-0008-1461-4
Abstract
A His-rich domain of preCollagen-D found in byssal threads is derivatized with Cys and Dopa flanks to allow for mussel-inspired polymerization. Artificial mussel glue proteins are accessed that combine cysteinyldopa for adhesion with sequences for pH or Zn2+ induced β-sheet formation. The artificial constructs show strong adsorption to Al2O3, the resulting coatings tolerate hypersaline conditions and cohesion is improved by activating the β-sheet formation, that enhances E-modulus up to 60%.