  We report how the electron transport through a solid-state metal/Gly-Gly-His
tripeptide (GGH) monolayer/metal junction and the metal/GGH work function are
modified by the GGH complexation with Cu2+ ions. Conducting AFM is used to
measure the current-voltage histograms. The work function is characterized by
combining macroscopic Kelvin probe and Kelvin probe force microscopy at the
nanoscale. We observe that the Cu2+ ions complexation with the GGH monolayer is
highly dependent on the molecular surface density and results in opposite
trends. In the case of a high density monolayer the conformational changes are
hindered by the proximity of the neighboring peptides, hence forming an
insulating layer in response to copper-complexation. Whereas the slightly lower
density monolayers allow for the conformational change to a looped peptide
wrapping the Cu-ion, which results in a more conductive monolayer. Copper-ion
complexation to the high- and low-density monolayers systematically induces an
increase of the work functions. Copper-ion complexation to the low-density
monolayer induces an increase of electron transport efficiency, while the
copper-ion complexation to the high-density monolayer results in a slight
decrease of electron transport. Both of the observed trends are in agreement
with first-principle calculations. Complexed copper to low density
GGH-monolayer induces a new gap state slightly above the Au Fermi energy that
is absent in the high density monolayer.
