Temperature induced conformational changes in the elastin-like peptide GVG(VPGVG)3
Author:
Affiliation:
1. Institut für Festkörperphysik
2. Technische Universität Darmstadt
3. 64289 Darmstadt
4. Germany
5. Institut Laue-Langevin
6. 38000 Grenoble
7. France
8. Clemens-Schöpf-Institut für Organische Chemie und Biochemie
9. 64287 Darmstadt
Abstract
The elastin-like peptide displays conformational changes and aggregation upon heating, showing a collapsed conformation around the ITT for low concentration.
Funder
Deutsche Forschungsgemeinschaft
Publisher
Royal Society of Chemistry (RSC)
Subject
Condensed Matter Physics,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2019/SM/C9SM00583H
Reference37 articles.
1. Characterization of the Temperature- and Pressure-Induced Inverse and Reentrant Transition of the Minimum Elastin-Like Polypeptide GVG(VPGVG) by DSC, PPC, CD, and FT-IR Spectroscopy
2. Reduction-driven polypeptide folding by the ΔTt mechanism
3. Elastin: a representative ideal protein elastomer
4. Folding and Unfolding of an Elastinlike Oligopeptide: “Inverse Temperature Transition,” Reentrance, and Hydrogen-Bond Dynamics
5. Elastin-like polypeptides and their applications in anticancer drug delivery systems: a review
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