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Zeitschrift für Physikalische Chemie

International journal of research in physical chemistry and chemical physics

Editor-in-Chief: Rademann, Klaus


IMPACT FACTOR 2018: 0.975
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2196-7156
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Volume 232, Issue 7-8

Issues

Elastin-like Peptide in Confinement: FT-IR and NMR T1 Relaxation Data

Susann Weißheit
  • Clemens-Schöpf-Institut für Organische Chemie und Biochemie, Technische Universität Darmstadt, Alarich-Weiss-Str. 16, 64287 Darmstadt, Germany
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/ Marie Kahse
  • Physical Chemistry I – Biophysical Chemistry, Faculty of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn-Str. 4a, 44227 Dortmund, Germany
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/ Kerstin Kämpf
  • Institut für Festkörperphysik, Technische Universität Darmstadt, Hochschulstr. 6, 64289 Darmstadt, Germany
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/ Alesia Tietze
  • Clemens-Schöpf-Institut für Organische Chemie und Biochemie, Technische Universität Darmstadt, Alarich-Weiss-Str. 16, 64287 Darmstadt, Germany
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/ Michael Vogel
  • Institut für Festkörperphysik, Technische Universität Darmstadt, Hochschulstr. 6, 64289 Darmstadt, Germany
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/ Roland Winter
  • Physical Chemistry I – Biophysical Chemistry, Faculty of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn-Str. 4a, 44227 Dortmund, Germany
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/ Christina Marie Thiele
  • Corresponding author
  • Clemens-Schöpf-Institut für Organische Chemie und Biochemie, Technische Universität Darmstadt, Alarich-Weiss-Str. 16, 64287 Darmstadt, Germany
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Published Online: 2018-06-14 | DOI: https://doi.org/10.1515/zpch-2017-1047

Abstract

We employed FT-IR and NMR experiments to investigate the influence of a cell-mimicking crowding environment on the structure and dynamics of an elastin-like peptide (ELP) with the sequence GVG(VPGVG)3, which – due to a high number of hydrophobic amino acid side chains – exhibits an inverse temperature transition (ITT). As simplified crowding agent, we used 30 wt% Ficoll. The FT-IR data revealed the well-known broad ITT above ~25°C, as observed by the decrease of the relative population of random coil structures and the concomitant increase of type II β-turns. Interestingly, the addition of Ficoll leads to a destabilizing effect of type II β-turn structures. This is in contrast to the expected excluded-volume effect of the macromolecular crowder, but can be explained by weak interactions of the peptide with the polysaccharide chains of the crowding agent. Further, the crowding agent leads to the onset of a reversal of the folding transition at high temperatures. The full assignment of the ELP allowed for a residue-specific investigation of the dynamic behavior of ELP by NMR. Due to a strong change of microscopic viscosity between native/buffered conditions and crowded conditions, relaxation data remain inconclusive with respect to the observation of an ITT. Hence, no quantitative details in terms of internal conformational changes can be obtained. However, temperature dependent differences in the 13C relaxation behavior between core and terminal parts of the peptide indicate temperature induced changes in the internal dynamics with generally higher internal mobility at chain ends: This is in full agreement with FT-IR data. In harmony with the FT-IR analysis, macromolecular crowding does not lead to significant changes in the relaxation behavior.

This article offers supplementary material which is provided at the end of the article.

Keywords: conformational dynamics; elastin-like peptide; FT-IR; macromolecular crowding; NMR-spectroscopy

References

About the article

Received: 2017-10-13

Accepted: 2018-05-17

Published Online: 2018-06-14

Published in Print: 2018-07-26


Citation Information: Zeitschrift für Physikalische Chemie, Volume 232, Issue 7-8, Pages 1239–1261, ISSN (Online) 2196-7156, ISSN (Print) 0942-9352, DOI: https://doi.org/10.1515/zpch-2017-1047.

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[2]
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