Charge migration for electron transfer via the polypeptide matrix of proteins is a key process in biological energy conversion and signaling systems. It is sensitive to the sequence of amino acids composing the protein and, therefore, offers a tool for chemical control of charge transport across biomaterial-based devices. We designed a series of linear oligoalanine peptides with a single tryptophan substitution that acts as a "dopant," introducing an energy level closer to the electrodes' Fermi level than that of the alanine homopeptide. We investigated the solid-state electron transport (ETp) across a selfassembled monolayer of these peptides between gold contacts. The single tryptophan "doping" markedly increased the conductance of the peptide chain, especially when its location in the sequence is close to the electrodes. Combining inelastic tunneling spectroscopy, UV photoelectron spectroscopy, electronic structure calculations by advanced density-functional theory, and dc current-voltage analysis, the role of tryptophan in ETp is rationalized by charge tunneling across a heterogeneous energy barrier, via electronic states of alanine and tryptophan, and by relatively efficient direct coupling of tryptophan to a Au electrode. These results reveal a controlled way of modulating the electrical properties of molecular junctions by tailormade "building block" peptides. oligopeptide | electron transport | self-assembled monolayer | inelastic electron tunneling spectroscopy | doping E lectron transfer (ET) processes taking place between prosthetic groups across the polypeptide matrices of proteins (1-3) have been extensively explored by, e.g., time-resolved photolysis (4, 5), pulse radiolysis (6, 7), scanning tunneling microscopy (8, 9), electrochemical methods (10-12), and by theoretical studies (13-16). The surprisingly fast and efficient ET over considerable distances (up to ∼25 Å) (17) via peptide matrices in proteins suggests possible development of peptide-and protein-based bioelectronics with diverse functionality and relative ease of modification (18,19). Studying electron transport (ETp) via solid-state molecular junctions represents an approach, bridging the study of basic ET-related phenomena and electronic devices, where measuring ET rates as a function of an electrochemical driving force is replaced by measuring current across molecular junctions as a function of an applied electrical voltage (20). Combining the concepts and methods of molecular electronics such as currentvoltage (I-V) line-shape analysis (21, 22), temperature-dependent measurements (23, 24), and electronic spectroscopy techniques (25-27) may yield new insights into the mechanism of ETp across the peptide matrix of proteins (28-30) and pave the road to peptide-and protein-based electronic devices for switching, rectification, and memory (18, 31).ETp via homopeptides has been investigated, probing the roles of specific amino acid residues, their protonation, and secondary structure (29,32). Synthetic heteropeptides with defined compositi...