AI Article Synopsis
- The tripeptide glycyl-histidyl-glycine (GHG) can form strong hydrogels at concentrations over 40 mM when its imidazole group is deprotonated.
- The gel exhibits a storage modulus (G') of around 50 kPa, indicating its structural strength.
- Spectroscopic analysis shows that the gel phase contains both helically twisted β-sheets and individual monomer units coexisting together.
Article 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.
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| http://dx.doi.org/10.1039/d0sm00224k | DOI Listing |
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