Molecular design principles of Lysine-DOPA wet adhesion.

ABSTRACT: The mussel byssus has long been a source of inspiration for the adhesion community. Recently, adhesive synergy between flanking lysine (Lys, K) and 3,4-Dihydroxyphenylalanine (DOPA, Y) residues in the mussel foot proteins (Mfps) has been highlighted. However, the complex topological relationship of DOPA and Lys as well as the interfacial adhesive roles of other amino acids have been understudied. Herein, we study adhesion of Lys and DOPA-containing peptides to organic and inorganic substrates using single-molecule force spectroscopy (SMFS). We show that a modest increase in peptide length, from KY to (KY)₃, increases adhesion strength to TiO_2. Surprisingly, further increase in peptide length offers no additional benefit. Additionally, comparison of adhesion of dipepti

SUBMITTER: Li Y 

PROVIDER: S-EPMC7403305 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature