High affinity metal-oxide binding peptides with reversible binding

Abstract

A dodecamer peptide, and its modified variant, having a repeating glycine-lysine sequence was created and formed to bind with high affinity to oxide surfaces and certain activated polymeric surfaces. Reversible binding characteristics of the peptides were demonstrated. The peptides were integrated with proteins, cells and fusion proteins to provide attachment of the proteins, cells and fusion proteins to solid material structures. The peptides can be used to functionalize surfaces of components within mechanical, biomechanical, micro fluid, electronic, bio electronic, bio-optical, and biochemical devices. Experiments were canied out to assess functionalization and reusability of a suspended mass resonator's cantilever.

Dependencies are inferred from the claim text.