Stereochemistry underlies structure-function relationships across biology and materials science, ranging from proteins to electronic and spintronic materials. In this work, we investigate the electron transport properties of different oligopeptide stereoisomers using experiments and computational modeling. Single-molecule electronic experiments show that stereochemical modifications in tyrosine-based peptides lead to significant variations in molecular conductance along the peptide backbone due to enhanced stacking interactions and electronic coupling of aromatic side chains. In addition, stereochemical variations in alanine-based peptides give rise to changes in conductivity due to secondary structure interactions arising from {beta}-turn conformations. All-atom molecular dynamics (MD) simulations and quantum mechanical calculations are used to understand the molecular origins of the effect of stereochemistry on the structural and electronic properties of peptides. Overall, this work shows that stereochemical modification of non-terminal amino acids effectively controls electron transport due to aromatic side chain interactions or secondary structure effects. These insights open new avenues for the molecular design of peptide-based electronic materials with enhanced function.
Samajdar, R., Chhabra, H., Meigooni, M., Yi, S., Liu, X., Wu, J. L., Tajkhorshid, E., Schroeder, C. M.
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