Adhesion of DOPA-functionalized model membranes to hard and soft surfaces

Murat Guvendiren, David Brass, Phillip B. Messersmith, Kenneth R. Shull

Research output: Contribution to journalArticlepeer-review

71 Scopus citations


The adhesive proteins secreted by marine mussels form a natural glue that cures rapidly to form strong and durable bonds in aqueous environments. These mussel adhesive proteins contain an unusual amino acid, 3,4-dihydroxy-L-phenylalanine (DOPA), which is largely responsible for their cohesive and adhesive strengths. In this study, we incorporated DOPA into diblock and triblock polymers and developed a membrane contact experiment to assess the adhesive interactions of these materials with TiO2 and tissue surfaces. In a typical experiment a micrometer-thick DOPA-functionalized elastomeric membrane is attached to the end of a cylindrical glass tube. Application of a positive pressure to the tube brings the membrane into contact with the surface of interest. The negative pressure needed to separate the membrane from the substrate is a measure of the strength of the adhesive interaction. The test confirms previous results obtained with TiO2 substrates. Because the membrane geometry is well suited for rough or chemically heterogeneous surfaces, it is ideal for studies of tissue adhesion. DOPA was found to give strong adhesion to tissue surfaces, with the strongest adhesion obtained when the DOPA groups were oxidized while in contact with the tissue surface.

Original languageEnglish (US)
Pages (from-to)631-645
Number of pages15
JournalJournal of Adhesion
Issue number9
StatePublished - 2009
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • Mechanics of Materials
  • Surfaces and Interfaces
  • Surfaces, Coatings and Films
  • Materials Chemistry


  • Block Copolymers
  • DOPA
  • Marine Mussel Mimetics
  • Membrane
  • Tissue Adhesion


Dive into the research topics of 'Adhesion of DOPA-functionalized model membranes to hard and soft surfaces'. Together they form a unique fingerprint.

Cite this