Primary structure, thermodynamics, and function of self-assembled π-conjugated oligopeptides

Engineered self-assembling peptides offer a promising approach for the fabrication of novel macromolecular materials with applications as far reaching as drug delivery, antimicrobials, and regenerative medicine. Synthetic oligopeptides containing embedded π-conjugated subunits have been demonstrated to assemble β-sheet-like 1D ribbons with electronic and photophysical functionality, making them promising candidates as biocompatible organic electronics. An in-depth understanding of the relationship between peptide chemistry, molecular thermodynamics, and photophysical function of peptide aggregates can enable rational design of peptides tailored to specific applications. In this work, we conduct atomistic molecular simulations of assembly for an ensemble of peptide chemistries and use these data to train and validate a quantitative structure-property relationship (QSPR) relating peptide sequence to structural alignment and photophysical function. We use the QSPR model to perform high-throughput traversal of peptide sequence space to identify and test promising candidates for experimental fabrication.