Journal article
The tripeptide GHG as an unexpected hydrogelator triggered by imidazole deprotonation
Soft matter, Vol.16(17), pp.4110-4114
07 May 2020
PMID: 32322858
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The tripeptide glycyl-histidyl-glycine (GHG) self-assembles into long, crystalline fibrils forming a strong hydrogel (G ' similar to 50 kPa) above a critical concentration of 40 mM upon the deprotonation of its imidazole group. Spectroscopic data reveal a mixture of helically twisted beta -sheets and monomers to coexist in the gel phase.
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Details
- Title
- The tripeptide GHG as an unexpected hydrogelator triggered by imidazole deprotonation
- Creators
- Morgan L. Hesser - Drexel UniversityLavenia Thursch - Drexel UniversityTodd Lewis - Drexel UniversityDavid Diguiseppi - Drexel UniversityNicolas J. Alvarez - Drexel UniversityReinhard Schweitzer-Stenner - Drexel University
- Publication Details
- Soft matter, Vol.16(17), pp.4110-4114
- Publisher
- Royal Soc Chemistry
- Number of pages
- 5
- Grant note
- Steinbright Career Development Center of Drexel University DMR-170770; DMR-1915781 / National Science Foundation; National Science Foundation (NSF)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemical and Biological Engineering; [Retired Faculty]
- Identifiers
- 991019167844604721
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- Web of Science research areas
- Chemistry, Physical
- Materials Science, Multidisciplinary
- Physics, Multidisciplinary
- Polymer Science