Journal article
The impact of thermal history on the structure of glycylalanylglycine ethanol/water gels
Journal of peptide science, v 27(5), e3305
May 2021
PMID: 33619869
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
This work revisits several open questions regarding the mechanisms of GAG fibril formation and structure as a function of temperature. The authors recently hypothesized that there is a solubility limit of GAG in ethanol/water that induces self‐assembly. In other words, not all peptides can participate in fibrillization and some fraction is still soluble in solution. We show via FTIR spectroscopy that, indeed, free peptides are still present in solution after fibril formation, strongly supporting the solubility model. Furthermore, previous work showed GAG self‐assembled into right‐handed (phase I) or left‐handed (phase II) chiral structures depending on temperature. In this study, we analyze the crystalline structure of phase I and II gels via WAXS and SAXS to compare their crystalline structures and order. Rheological measurements were used to investigate the response of the fibrillar network to temperature. They reveal that the ability of the peptide to self‐assemble depends on the solubility at a given temperature and not on thermal history. Furthermore, the gel softening point, the linear viscoelastic gel microstructure, and relaxation spectrum are very similar between phase I and phase II. Overall, the temperature only affects the chirality of the fibrils and the formation kinetics.
The peptide Glycine‐Alanine‐Glycine (GAG) forms a fibrillar gel network in the presence of water and ethanol. Through thermal studies, we validate the hypothesis of a peptide self‐assembly underlined by a solubility mechanism. The solubility can be manipulated with temperature to reverse the chirality of the peptide fibrils and control gelation kinetics while the crystalline structure remains identical.
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Details
- Title
- The impact of thermal history on the structure of glycylalanylglycine ethanol/water gels
- Creators
- Lavenia J. Thursch - Drexel UniversityThamires A. Lima - Drexel UniversityReinhard Schweitzer‐Stenner - Drexel UniversityNicolas J. Alvarez - Drexel University
- Publication Details
- Journal of peptide science, v 27(5), e3305
- Publisher
- Wiley
- Number of pages
- 9
- Grant note
- National Science Foundation (USA) (DMR‐1707770)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemical and Biological Engineering; Chemistry
- Web of Science ID
- WOS:000620332200001
- Scopus ID
- 2-s2.0-85101211665
- Other Identifier
- 991019167517004721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Chemistry, Analytical