Terahertz spectroscopy for interpreting the formation and hierarchical structures of silk fibroin oligopeptides

Determining the configuration and conformation of peptides is crucial for interpreting their structure-property relationships. In this work, we present nondestructive terahertz time-domain spectroscopy combined with density functional theory (DFT) and potential energy distribution (PED) analysis to identify the hierarchical structures of oligopeptides. The characteristic THz spectra of silk fibroin oligopeptides have been measured. Supported by DFT and PED analysis, the intrinsic differences among the dipeptides were identified by the collective vibrational modes of "R" groups and terminal groups linked by molecular chains of amido bonds or benzene rings. For tetrapeptides and hexapeptides, a few weak resonances and intensity differences were distinguished by the vibration mode of the molecular collective network formed by the interaction of amide planes and intramolecular hydrogen bond interactions. According to the THz absorption analyses of amide planes and intramolecular interactions within the molecular chains of silk fibroin oligopeptide isomer pairs, the formation and hierarchical structures were successfully interpreted using THz spectroscopy. This investigation develops a better understanding of the peptide formation mechanism, which further provides guidance in interpreting the formation of silk.