Amino acids are the most simplistic bio-building blocks and perform a variety of functions in metabolic activities. Increasing publications report that amino acid-based superstructures present amyloid-like characteristics, arising from their supramolecular β-sheet secondary structures driven by hydrogen-bonding-connected supramolecular β-strands, which are formed by head-to-tail hydrogen bonds between terminal amino and carboxyl groups of the adjacent residues. Therefore, the establishment of the structure-function relationships is critical for exploring the properties and applications of amino acid assemblies. Among the naturally encoded self-assembling amino acids, tyrosine (Y)-based superstructures have been found to show diverse properties and functions including high rigidity, promoting melanin formations, mood regulations, and preventing anxiety, thus showing promising potential as next-generation functional biomaterials for biomedical and bio-machine interface applications. However, the development of Y-based organizations of functional features is severely limited due to the intrinsic difficulty of modulating the energetically stable supramolecular β-sheet structures. Herein, we report that by the racemic assembly of l-Y and d-Y, the supramolecular secondary structures are modulated from the antiparallel β-sheets in the enantiomeric assemblies to the parallel ones in the racemate counterparts, thus leading to higher degrees of freedom, which finally induce distinct organization kinetics and modulation of the physicochemical properties including the optical shifts, elastic softening, and the piezoelectric outputs of the superstructures.
Keywords: amino acids; molecular manufacturing; property modulations; racemic assembly; supramolecular β-sheets.