1. Peptide Length and Dopa Determine Iron‐Mediated Cohesion of Mussel Foot Proteins
- Author
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Das, Saurabh, Martinez Rodriguez, Nadine R, Wei, Wei, Waite, J Herbert, and Israelachvili, Jacob N
- Subjects
Chemical Sciences ,Dopa ,Mussel Foot Protein ,bio-adhesion ,coating proteins ,iron chelation ,mfp-1 peptide ,Physical Sciences ,Engineering ,Materials ,Chemical sciences ,Physical sciences - Abstract
Mussel adhesion to mineral surfaces is widely attributed to 3,4-dihydroxyphenylalanine (Dopa) functionalities in the mussel foot proteins (mfps). Several mfps, however, show a broad range (30-100%) of Tyrosine (Tyr) to Dopa conversion suggesting that Dopa is not the only desirable outcome for adhesion. Here, we used a partial recombinant construct of mussel foot protein-1 (rmfp-1) and short decapeptide dimers with and without Dopa and assessed both their cohesive and adhesive properties on mica using a surface forces apparatus (SFA). Our results demonstrate that at low pH, both the unmodified and Dopa-containing rmfp-1s show similar energies for adhesion to mica and self-self interaction. Cohesion between two Dopa-containing rmfp-1 surfaces can be doubled by Fe3+ chelation, but remains unchanged with unmodified rmfp-1. At the same low pH, the Dopa modified short decapeptide dimer did not show any change in cohesive interactions even with Fe3+. Our results suggest that the most probable intermolecular interactions are those arising from electrostatic (i.e., cation-π) and hydrophobic interactions. We also show that Dopa in a peptide sequence does not by itself mediate Fe3+ bridging interactions between peptide films: peptide length is a crucial enabling factor.
- Published
- 2015