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Updated: Jul 17, 2026

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels
Published on: September 6, 2024
Stabilization of peptide fibrils by hydrophobic interaction
Joris T Meijer1, Marjolijn Roeters, Valentina Viola
1Organic Chemistry, Institute for Molecules and Materials and Center for Molecular and Biomolecular Informatics, NCMLS, Radboud University Nijmegen, Toernooiveld 1- Huygens Building 03.016, 6525 ED Nijmegen, The Netherlands.
Abstract:
Hydrophobic interactions play an important role in assembly processes in aqueous environments. In case of peptide amphiphiles, hydrophobicity is combined with hydrogen bonding to yield well-defined peptide-based aggregates. Here, we report a systematic study after the role of hydrophobic interactions on both stabilization and morphology of a peptide fibrillar assembly. For this purpose, alkyl tails were connected to a known beta-sheet forming peptide with the sequence KTVIIE. The introduction of n-alkyl groups induced thermal stability to the assemblies without affecting the morphology of the peptide aggregates.
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