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Tuesday, 06 May 2014

Explaining mussel’s adhesion to substrates at the nanoscale

Relevant factors governing the adhesion of catechol groups in model systems may help design new protective coatings and powerful wet adhesives.

The remarkable adhesion to substrates shown by mussel byssus proteins has been mainly attributed to the presence of significant amounts of catechol-like tyrosine in their sequences. A work published recently in Small, and selected to illustrate the issue cover, uses a nanostructured model to better understand the adhesion force of catecholic groups. Knowledge of the molecular and structural factors involved in catechol-mediated adhesion could be useful to design new protective coatings and powerful adhesives for wet environments.

The work was coordinated by the ICN2 Nanostructured Functional Materials group (Nanosfun), led by the Group Leader Dr. Daniel Ruiz-Molina, and included researchers from other ICN2 teams, the Department of Chemistry of the Universitat Autonoma de Barcelona (UAB), the Institut de Ciencia de Materials de Barcelona (ICMAB-CSIC) and the Instituto de Ciencia Molecular (ICMol-Universidad de Valencia).

The main focus of the study is the measure of the retraction force of an Atomic Force Microscopy tip in contact with the upward-facing catechol rings of a model compound, self-assembled in an ordered monolayer bound to an epitaxial gold surface via a thiol group. The results highlight the importance of spatial and chemical order in catecholic layers with regard to enhanced adhesion.


Article Reference:

Guardingo, M., Bellido, E., Miralles-Lluma, R., Faraudo, J., Sedó, J., Tatay, S., Verdaguer, A., Busqué, F. and Ruiz-Molina, D. (2014), Self-Assembled Monolayers: Bioinspired Catechol-Terminated Self-Assembled Monolayers with Enhanced Adhesion Properties (Small 8/2014). Small, 10: 1656. doi: 10.1002/smll.201470049 http://onlinelibrary.wiley.com/doi/10.1002/smll.201470049/abstract