Enzymatic polymerization of enantiomeric L-3,4-dihydroxyphenylalanine into films with enhanced rigidity and stability

(L)-3,4-dihydroxyphenylalanine is an important molecule in the adhesion of mussels, and as an oxidative precursor of natural melanin, it plays an important role in living system. Here, we investigate the effect of the molecular chirality of 3,4-dihydroxyphenylalanine on the properties of the self-assembled films by tyrosinase-induced oxidative polymerization. The kinetics and morphology of pure enantiomers are completely altered upon their co-assembly, allowing the fabrication of layer-to-layer stacked nanostructures and films with improved structural and thermal stability. The different molecular arrangements and self-assembly mechanisms of the (L+D)-racemic mixtures, whose oxidation products have increased binding energy, resulting in stronger intermolecular forces, which significantly increases the elastic modulus. This study provides a simple pathway for the fabrication of biomimetic polymeric materials with enhanced physicochemical properties by controlling the chirality of monomers. (L)-3,4-Dihydroxyphenylalanine plays an important role in living system. Here, the authors investigated the effect of the molecular chirality of (L)-3,4-dihydroxyphenylalanine on the improved structural and thermal stability of self-assembled films by tyrosinase-induced oxidative polymerization.

Automated summary

The authors investigated the effect of the molecular chirality of (L)-3,4-dihydroxyphenylalanine on the improved structural and thermal stability of self-assembled films by tyrosinase-induced oxidative polymerization. The pure enantiomers showed altered kinetics and morphology upon co-assembly, allowing the fabrication of layer-to-layer stacked nanostructures and films with enhanced properties. The (L+D)-racemic mixtures exhibited different molecular arrangements and self-assembly mechanisms, resulting in stronger intermolecular forces and increased elastic modulus.