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

Susann Weißheit; Marie Kahse; Kerstin Kämpf; Alesia Tietze; Michael Vogel; Roland Winter; Christina Marie Thiele

doi:10.1515/zpch-2017-1047

Published by De Gruyter (O) June 14, 2018

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

Susann Weißheit , Marie Kahse , Kerstin Kämpf , Alesia Tietze , Michael Vogel , Roland Winter and Christina Marie Thiele

From the journal Zeitschrift für Physikalische Chemie

https://doi.org/10.1515/zpch-2017-1047

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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.

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

Acknowledgements

The authors thank Volker Schmidts and Julian Ilgen for helpful discussions about the NMR measurements and data. Additionally, thanks to Michaela Standhardt for support with the first T₁ measurements. We thank Satyajit Patra for carrying out the FCS measurements and Melanie Berghaus for the SAXS data on ELP. The Deutsche Forschungsgemeinschaft (DFG) is thanked for funding in the framework of FOR1583 through projects DFG TH 1115/8-1, WI 742/17-1/2 and VO 905/8-1/2.

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Supplementary Material:

The online version of this article offers supplementary material (https://doi.org/10.1515/zpch-2017-1047).

Received: 2017-10-13

Accepted: 2018-05-17

Published Online: 2018-06-14

Published in Print: 2018-07-26