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Concentration Dependence of a Hydrogel Phase Formed by the Deprotonation of the Imidazole Side Chain of Glycylhistidylglycine
Journal article   Peer reviewed

Concentration Dependence of a Hydrogel Phase Formed by the Deprotonation of the Imidazole Side Chain of Glycylhistidylglycine

Morgan Hesser, Lavenia J. Thursch, Todd R. Lewis, Thamires A. Lima, Nicolas J. Alvarez and Reinhard Schweitzer-Stenner
Langmuir, v 37(23), pp 6935-6946
15 Jun 2021
PMID: 34077210

Abstract

Chemistry Chemistry, Multidisciplinary Chemistry, Physical Materials Science Materials Science, Multidisciplinary Physical Sciences Science & Technology Technology
Upon deprotonation of its imidazole group at similar to pH 6, the unblocked tripeptide glycylhistidylglycine (GHG) self-assembles into very long crystalline fibrils on a 10-1000 mu m scale which are capable of forming a volume spanning network, that is, hydrogel. The critical peptide concentration for self-assembly at a pH of 6 mM lies between 50 and 60 The fraction of peptides that self-assemble into fibrils depends on the concentration of deprotonated GHG. While IR spectra seem to indicate the formation of fibrils with standard amyloid fibril beta-sheet structures, vibrational circular dichroism spectra show a strongly enhanced amide I' signal, suggesting that the formed fibrils exhibit significant chirality. The fibril chirality appears to be a function of peptide concentration. Rheological measurements reveal that the rate of gelation is concentration-dependent and that there is an optimum gel strength at intermediate peptide concentrations of ca. 175 mM. This paper outlines the unique properties of the GHG gel phase which is underlain by a surprisingly dense fibril network with an exceptionally strong modulus that make them potential additives for biomedical applications.

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Web of Science research areas
Chemistry, Multidisciplinary
Chemistry, Physical
Materials Science, Multidisciplinary
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