Issue 17, 2020
From the journal:

Soft Matter

The tripeptide GHG as an unexpected hydrogelator triggered by imidazole deprotonation†

Morgan Hesser,a   Lavenia Thursch,b   Todd Lewis,b   David DiGuiseppi, ORCID logo a   Nicolas J. Alvarez ORCID logo *b  and  Reinhard Schweitzer-Stenner ORCID logo *a  

* Corresponding authors

a Department of Chemistry, Drexel University, 3141 Chestnut Street, Philadelphia, PA 19104, USA
E-mail: rschweitzer-stenner@drexel.edu

b Department of Chemical and Biological Engineering, Drexel University, 3141 Chestnut Street, Philadelphia, PA 19104, USA

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.

Graphical abstract: The tripeptide GHG as an unexpected hydrogelator triggered by imidazole deprotonation

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Article information

DOI
https://doi.org/10.1039/D0SM00224K
Article type
Communication
Submitted
08 Feb 2020
Accepted
06 Apr 2020
First published
09 Apr 2020

Soft Matter, 2020,16, 4110-4114

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The tripeptide GHG as an unexpected hydrogelator triggered by imidazole deprotonation

M. Hesser, L. Thursch, T. Lewis, D. DiGuiseppi, N. J. Alvarez and R. Schweitzer-Stenner, Soft Matter, 2020, 16, 4110 DOI: 10.1039/D0SM00224K

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