The tripeptide GHG as an unexpected hydrogelator triggered by imidazole deprotonation
Morgan Hesser, Lavénia Thursch, Todd R. Lewis, David DiGuiseppi, Nicolas J. Alvarez, Reinhard Schweitzer‐Stenner
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 β-sheets and monomers to coexist in the gel phase.
Topics & Concepts
TripeptideImidazoleDeprotonationChemistryGlycineStereochemistryOrganic chemistryPeptideBiochemistryAmino acidIonSupramolecular Self-Assembly in MaterialsPolydiacetylene-based materials and applicationsPhotochromic and Fluorescence Chemistry