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Related Experiment Video

Updated: Jun 27, 2026

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

Supramolecular gel formation and self-correction induced by aggregation-driven conformational changes.

Francisco Rodríguez-Llansola¹, Juan F Miravet, Beatriu Escuder

¹Universitat Jaume I, Dpt. Química Inorgànica i Orgànica, 12071, Castelló, Spain.

Chemical Communications (Cambridge, England)

|December 23, 2008

Summary

Low molecular weight peptidomimetics form self-assembled fibrillar networks. These networks, formed via an unfolding process, can correct from kinetic to thermodynamic stability.

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Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels

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Published on: September 6, 2024

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Last Updated: Jun 27, 2026

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

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Published on: August 2, 2012

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels

Published on: September 6, 2024

Area of Science:

Supramolecular Chemistry
Materials Science
Biomaterials

Background:

Low molecular weight compounds can self-assemble into ordered structures.
Peptidomimetics offer tunable properties for advanced materials.
Understanding aggregation mechanisms is crucial for designing functional soft materials.

Purpose of the Study:

To investigate the self-assembly of peptidomimetics with a Pro-Val moiety into fibrillar networks.
To elucidate the aggregation mechanism, including the role of unfolding.
To explore the self-correction of kinetically formed networks into thermodynamically stable states.

Main Methods:

Synthesis of low molecular weight peptidomimetics.
Characterization of self-assembled fibrillar networks using techniques like microscopy and spectroscopy.
Analysis of the aggregation mechanism through kinetic and thermodynamic studies.

Main Results:

Successful formation of self-assembled fibrillar networks from peptidomimetics.
Identification of an unfolding process associated with fibril formation.
Demonstration of self-correction from kinetically controlled to thermodynamically stable networks.

Conclusions:

Low molecular weight peptidomimetics are effective building blocks for self-assembled fibrillar networks.
The aggregation process involves molecular unfolding, leading to ordered structures.
Kinetically formed networks possess the ability to evolve into more stable thermodynamic states.