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Updated: Aug 18, 2025

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
Published on: February 6, 2020
Transition from continuous to microglobular shaped peptide assemblies through a Liesegang-like enzyme-assisted
Jean-Yves Runser1, Fatima Fneich2, Bernard Senger3
1Université de Strasbourg, CNRS, Institut Charles Sadron UPR 22, 67034 Strasbourg, France; Institut National de la Santé et de la Recherche Médicale, UMR-S 1121, "Biomatériaux et Bioingénierie", 67084 Strasbourg, France; Université de Strasbourg, Faculté de Chirurgie Dentaire, Fédération de Médecine Translationnelle de Strasbourg (FMTS), and Fédération des Matériaux et Nanoscience d'Alsace (FMNA), 67000 Strasbourg, France.
Abstract:
Enzyme-assisted self-assembly confined within host materials leads to Liesegang-like spatial structuration when precursor peptides are diffusing through an enzyme-functionalized hydrogel. It is shown here that playing on peptide and enzyme concentrations results in a transition from continuous self-assembled peptide areas to individual microglobules. Their morphology, location, size and buildup mechanism are described. Additionally, it is also found that the enzymes adsorb onto the peptide self-assemblies leading to co-localization of peptide self-assembled microglobules and enzymes. Finally, we find that large microglobules grow at the expense of smaller ones present in their vicinity in a kind of Ostwald ripening process, illustrating the dynamic nature of the peptide self-assembly process within host hydrogels.
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