Journal article
Demixing of water and ethanol causes conformational redistribution and gelation of the cationic GAG tripeptide
Chemical communications (Cambridge, England), v 51(92), pp 16498-16501
28 Nov 2015
PMID: 26414527
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The cationic tripeptide GAG undergoes three conformational changes in binary mixtures of water and ethanol. At 17 mol% of ethanol conformational sampling is shifted from pPII towards β-strands. A more pronounced shift in the same direction occurs at 40 mol%. At ca. 55 mol% of ethanol and above a peptide concentration of ca. 0.2 M the ternary peptide-water-ethanol mixture forms a hydrogel which is comprised of unusually large crystalline like non-β sheet fibrils forming a sample spanning matrix.
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Details
- Title
- Demixing of water and ethanol causes conformational redistribution and gelation of the cationic GAG tripeptide
- Creators
- Bridget Milorey - Drexel UniversityStefanie Farrell - Drexel UniversitySiobhan E Toal - University of PennsylvaniaReinhard Schweitzer-Stenner - Drexel University
- Publication Details
- Chemical communications (Cambridge, England), v 51(92), pp 16498-16501
- Publisher
- Royal Society of Chemistry
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]; Chemistry
- Web of Science ID
- WOS:000364819600011
- Scopus ID
- 2-s2.0-84946811454
- Other Identifier
- 991019168008804721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Chemistry, Multidisciplinary