Abstract
The tripeptide glycyl-histidyl-glycine (GHG) self-assembles into long, crystalline fibrils forming a strong hydrogel (G' ~ 50 kPa) above a critical concentration of 40 mM upon the deprotonation of its imidazole group. Spectroscopic data reveal a mixture of helically twisted ß-sheets and monomers to coexist in the gel phase.
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CITATION STYLE
APA
Hesser, M., Thursch, L., Lewis, T., DiGuiseppi, D., Alvarez, N. J., & Schweitzer-Stenner, R. (2020). The tripeptide GHG as an unexpected hydrogelator triggered by imidazole deprotonation. Soft Matter, 16(17), 4110–4114. https://doi.org/10.1039/d0sm00224k
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