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Resolving Non‐Specific and Specific Adhesive Interactions of Catechols at Solid/Liquid Interfaces at the Molecular Scale


The adhesive system of mussels evolved into a powerful and adaptive system with affinity to a wide range of surfaces. It is widely known that thereby 3,4‐dihydroxyphenylalanine (Dopa) plays a central role. However underlying binding energies remain unknown at the single molecular scale. Here, we use single‐molecule force spectroscopy to estimate binding energies of single catechols with a large range of opposing chemical functionalities. Our data demonstrate significant interactions of Dopa with all functionalities, yet most interactions fall within the medium–strong range of 10–20 kBT. Only bidentate binding to TiO2 surfaces exhibits a higher binding energy of 29 kBT. Our data also demonstrate at the single‐molecule level that oxidized Dopa and amines exhibit interaction energies in the range of covalent bonds, confirming the important role of Dopa for cross‐linking in the bulk mussel adhesive. We anticipate that our approach and data will further advance the understanding of biologic and technologic adhesives.

Biophysik: Wechselwirkungen zwischen Dopa‐Molekülen und Oberflächen sind in der Nanotechnologie und für die Modifizierung von Oberflächen wichtig (Dopa=3,4‐Dihydroxyphenylalanin). Die Bindungsenergie zwischen Dopa‐Molekülen und verschiedenen Oberflächen wurden mittels Einzelmolekül‐Kraftspektroskopie bestimmt (siehe Bild; ΔG=freie Energie und F=Kraft).

Authors:   Thomas Utzig, Philipp Stock, Markus Valtiner
Journal:   Angewandte Chemie
Volume:   128
edition:   33
Year:   2016
Pages:   9676
DOI:   10.1002/ange.201601881
Publication date:   04-Jul-2016
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