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

Yuhe Shen, Rongxin Su, Dongzhao Hao, Xiaojian Xu, Meital Reches, Jiwei Min, Heng Chang, Tao Yu, Qing Li, Xiaoyu Zhang, Yuefei Wang*, Yuefei Wang*, Wei Qi*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

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.

Original languageAmerican English
Article number3054
JournalNature Communications
Volume14
Issue number1
DOIs
StatePublished - Dec 2023

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© 2023, The Author(s).

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