The use of phage display to select
material-specific peptides provides
a general route towards modification and functionalization of surfaces
and interfaces. However, a rational structural engineering of the
peptides for optimal affinity is typically not feasible because of
insufficient structure−function understanding. Here, we investigate
the influence of multivalency of diamond-like carbon (DLC) binding
peptides on binding characteristics. We show that facile linking of
peptides together using different lengths of spacers and multivalency
leads to a tuning of affinity and kinetics. Notably, increased length
of spacers in divalent systems led to significantly increased affinities.
Making multimers influenced also kinetic aspects of surface competition.
Additionally, the multivalent peptides were applied as surface functionalization
components for a colloidal form of DLC. The work suggests the use
of a set of linking systems to screen parameters for functional optimization
of selected material-specific peptides