(228fc) Mimicking Mussel Adhesives with Peptide Glue

The development of glues that adhere to wet surfaces is important for medical, dental, and marine applications. However, glues that are effective in dry conditions often fail in aqueous conditions, especially in salt solutions or when the surfaces are contaminated, for example by a biofilm. Nevertheless, many marine organisms adhere to surfaces under water. The marine mussel attaches itself to rocks in the ocean by secreting proteins which adhere to fouled mineral surfaces via chemical and physical bonds. To study these interactions, a peptide glue was synthesized to mimic a common type of mussel adhesive protein (MFP-3). The adhesion energies between the peptide and hydrophobic (CH₃-SAM) and hydrophilic (OH-SAM, mica) surfaces were measured experimentally using a surface forces apparatus (SFA) and computed from molecular dynamics simulations. Changing surface hydrophobicity resulted in different peptide-surface molecular geometries, and suggested a synergistic and adaptive adhesion mechanism based on adjacent hydrophobic and hydrophilic residues. Understanding the dependence of peptide adhesion on peptide primary structure and interaction geometry will allow the design of adhesives for use in aqueous environments.