Expanding the bowknot-like morphological versatility in supramolecular assemblies of diphenylalanine

A small organic molecule caffeic acid (CA) was used to manipulate the self-assembly of diphenylalanine (FF) molecules. Bidirectional hierarchical morphology of typical bowknot-like assemblies was constructed through supramolecular co-assembly of FF and CA. By controlling the preparation condition, versatile bowknot-like structures could be exclusively obtained. The FTIR, XRD, UV and XPS results indicated the co-existence of the FF and CA components in the assembly. Intermolecular interaction of hydrogen bonding and π-π interaction between the FF and CA might be the primary driving force. This work provides novel bowknot-like structure of peptide which is rarely observed in biological molecules through a convenient co-assembly way. We believe that such manipulation may not only provide us with a deeper understanding of the principles of the dipeptide co-assembly process but also may enable us to construct more unprecedented peptide-based materials for comprehensive applications. [Display omitted] •A bowknot-like morphological of diphenylalanine was constructed.•The versatility of the bowknot-like structures has been acquired by the regulation of a small organic molecule caffeic acid.•Spectroscopy measurement confirmed the components of the assembly.