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arXiv · 2608.19810

A Central Disulfide Junction Drives Transient Network Formation in Elastin-Like Polypeptides, Enabling Low-Concentration Hydrogels

Abstract

The self-assembly of associative triblock copolymers composed of a central hydrophilic elastin-like polypeptide (ELP) block and short fatty acid end groups (C16) was investigated in aqueous solution. In one system, the ELP contains 80 pentapeptide units (C16-80-C16), whereas in the other two C16-ELP40 chains were oxidatively coupled through their terminal cysteine residues to form a central disulfide bond, yielding C16-(40)2-C16. Despite their nearly identical molecular weights and compositions, the two polymers exhibit markedly different self-assembly behaviors. C16-80-C16 forms large hydrophobic aggregates that remain kinetically trapped and do not develop a dynamically connected network. In contrast, C16-(40)2-C16 forms very small associative nodes with an aggregation number of only $\sim$3 chains. These nodes coexist with larger clusters and become dynamically interconnected at higher concentrations, leading to transparent hydrogels at concentrations as low as 2.5 wt %. Oscillatory rheology reveals a transient Maxwell network governed by a single relaxation process associated with the reversible association of the C16 end groups. SAXS, light scattering, cryo-TEM, and molecular modeling consistently support a model in which the central disulfide junction promotes transient network formation.

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Tingting Zhang, Jean-François Le Meins, Jean-Paul Chapel, Saron Catak, Guillaume Goudounet, Olivier Sandre, Nadia Mahmoudi, Christophe Schatz, Bertrand Garbay. 2026-08-20. A Central Disulfide Junction Drives Transient Network Formation in Elastin-Like Polypeptides, Enabling Low-Concentration Hydrogels. https://arxiv.org/abs/2608.19810

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