Sequence-defined positioning of amine and amide residues to control catechol driven wet adhesion

• Published in: Chemical science (Cambridge) Vol. 11; no. 36; pp. 9919 - 9924
• Main Authors: Fischer, Lukas, Strzelczyk, Alexander K, Wedler, Nils, Kropf, Christian, Schmidt, Stephan, Hartmann, Laura
• Format: Journal Article
• Language: English
• Published: CAMBRIDGE Royal Soc Chemistry 31.08.2020; Royal Society of Chemistry; The Royal Society of Chemistry
• Subjects: Adhesion; Adhesives; Amides; Catechol; Chemical analysis; Chemistry; Chemistry, Multidisciplinary; Functional groups; Hydrogels; Oligomers; Physical Sciences; Residues; Science & Technology; FUNCTIONALIZATION; POLYMERS; ENERGY; CONTACT; SINGLE-MOLECULE; MUSSEL; SYNERGY; DEPROTECTION; PROTEINS; SURFACE-CHEMISTRY
• ISSN: 2041-6520; 2041-6539
• DOI: 10.1039/d0sc03457f

Catechol and amine residues, both abundantly present in mussel adhesion proteins, are known to act cooperatively by displacing hydration barriers before binding to mineral surfaces. In spite of synthetic efforts toward mussel-inspired adhesives, the effect of positioning of the involved functional groups along a polymer chain is not well understood. By using sequence-defined oligomers grafted to soft hydrogel particles as adhesion probes, we study the effect of catechol-amine spacing, as well as positioning relative to the oligomer terminus. We demonstrate that the catechol-amine spacing has a significant effect on adhesion, while shifting their position has a small effect. Notably, combinations of non-charged amides and catechols can achieve similar cooperative effects on adhesion when compared to amine and catechol residues. Thus, these findings provide a blueprint for the design of next generation mussel-inspired adhesives. The catechol driven adhesion of precision macromolecules on glass surfaces is quantified by soft colloidal probe readout. Catechol moieties are shown to synergize with amine and amide residues depending on residue spacing and residue order.