Mechanical Enhancement and Kinetics Regulation of Fmoc‐Diphenylalanine Hydrogels by Thioflavin T

The self‐assembly of peptides is a key direction for fabrication of advanced materials. Novel approaches for fine tuning of macroscopic and microscopic properties of peptide self‐assemblies are of a high demand for constructing biomaterials with desired properties. In this work, while studying the k...

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Published in:Angewandte Chemie International Edition 2021-11, Vol.60 (48), p.25339-25345
Main Authors: Tikhonova, Tatiana N., Rovnyagina, Nataliya N., Arnon, Zohar A., Yakimov, Boris P., Efremov, Yuri M., Cohen‐Gerassi, Dana, Halperin‐Sternfeld, Michal, Kosheleva, Nastasia V., Drachev, Vladimir P., Svistunov, Andrey A., Timashev, Peter S., Adler‐Abramovich, Lihi, Shirshin, Evgeny A.
Format: Article
Language:English
Subjects:
Assembly
Biomaterials
biomechanics
Biomedical materials
Fabrication
Fibers
fluorescence lifetime
hydrogel
Hydrogels
Kinetics
Mechanical properties
peptide self-assembly
Peptides
Rigidity
Thermal stability
Thioflavin T
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Summary:The self‐assembly of peptides is a key direction for fabrication of advanced materials. Novel approaches for fine tuning of macroscopic and microscopic properties of peptide self‐assemblies are of a high demand for constructing biomaterials with desired properties. In this work, while studying the kinetics of the Fmoc‐Diphenylalanine (Fmoc‐FF) dipeptide self‐assembly using the Thioflavin T (ThT) dye, we observed that the presence of ThT strongly modifies structural and mechanical properties of the Fmoc‐FF hydrogel. Notably, the presence of ThT resulted in a tenfold increase of the gelation time and in the formation of short and dense fibers in the hydrogel. As a result of these morphological alteration higher thermal stability, and most important, tenfold increase of the hydrogel rigidity was achieved. Hence, ThT not only slowed the kinetics of the Fmoc‐FF hydrogel formation, but also strongly enhanced its mechanical properties. In this study, we provide a detailed description of the ThT effect on the hydrogel properties and suggest the mechanisms for this phenomenon, paving the way for the novel approach to the control of the peptide hydrogels’ micro‐ and macroscale properties. Thioflavin T dramatically enhances the structural and mechanical properties of the Fmoc‐FF hydrogel and drives the self‐assembly by interfering the metastable phase of the two‐step nucleation process.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.202107063