Self-Assembly and Gelation Study of Dipeptide Isomers with Norvaline and Phenylalanine

Dipeptides have emerged as attractive building blocks for supramolecular materials thanks to their low-cost, inherent biocompatibility, ease of preparation, and environmental friendliness they do not persist in the environment. In particular, hydrophobic amino acids are ideal candidates self-assembly polar green solvents, a certain level hydrophobicity is required favor aggregation reduce peptide solubility. this work, we analyzed ability self-assemble gel dipeptides based on norvaline (Nva) phenylalanine (Phe), studying all combinations yielding enantiomers, which display same physicochemical properties, hence behavior achiral environments those studied herein. A single-crystal X-ray diffraction compounds revealed fine details over molecular packing non-covalent interactions.