The byssal adhesion mechanism of the biofouling species Dreissena polymorpha was investigated using a combination of studies on synthetic peptide mimics of tandem repeat sequences from byssal component Dreissena polymorpha foot protein 1 (Dpfp-1) and characterization of the regions of the byssus. A 20-residue fusion peptide incorporating two Dpfp-1 repeat sequences adopts a random coil and β-turn conformation in solution, and spontaneously forms a film at the solid-liquid interface in the presence of iron (III) cations. Infrared characterization of the byssus Amide I region showed that β-sheets dominate its secondary structure, although the proportion of different secondary structures varies between regions. Matrix-assisted laser desorption ionization (MALDI) mass spectrometry of intact byssal regions identified previously unknown differences in the composition of byssal threads, plaques, and the adhesive interface, which are believed to correlate to the different roles of these components in the overall structure.

The byssal adhesion mechanism of the biofouling species Dreissena polymorpha was investigated using a combination of studies on synthetic peptide mimics of tandem repeat sequences from byssal component Dreissena polymorpha foot protein 1 (Dpfp-1) and characterization of the regions of the byssus. A 20-residue fusion peptide incorporating two Dpfp-1 repeat sequences adopts a random coil and β-turn conformation in solution, and spontaneously forms a film at the solid-liquid interface in the presence of iron (III) cations. Infrared characterization of the byssus Amide I region showed that β-sheets dominate its secondary structure, although the proportion of different secondary structures varies between regions. Matrix-assisted laser desorption ionization (MALDI) mass spectrometry of intact byssal regions identified previously unknown differences in the composition of byssal threads, plaques, and the adhesive interface, which are believed to correlate to the different roles of these components in the overall structure.