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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

C. Nicolini ^*, R. Ravindra ^*, B. Ludolph  and R. Winter ^*

^* Department of Chemistry, University of Dortmund, Dortmund, Germany; and Max-Planck Institute of Molecular Physiology, Dortmund, Germany

Correspondence: Address reprint requests to R. Winter, Dept. of Chemistry, Physical Chemistry I, University of Dortmund, Otto-Hahn Str. 6, D-44227 Dortmund, Germany. Tel.: 49-231-755-3900; E-mail: winter{at}pci.chemie.uni-dortmund.de.

We investigated the temperature- and pressure-dependent structure and phase behavior of a solvated oligopeptide, GVG(VPGVG), which serves as a minimalistic elastin-like model system, over a large region of the thermodynamic phase field, ranging from 2 to 120°C and from ambient pressure up to 10 kbar, applying various spectroscopic (CD, FT-IR) and thermodynamic (DSC, PPC) measurements. We find that this octapeptide behaves as a two-state system which undergoes the well-known inverse-temperature folding transition occurring at T 36°C, and, in addition, a slow trend reversal at higher temperatures, finally leading to a reentrant unfolding close to the boiling point of water. Furthermore, the pressure-dependence of the folding/unfolding transition was studied to yield a more complete picture of the p, T-stability diagram of the system. A molecular-level picture of these processes, in particular on the role of water for the folding and unfolding events of the peptide, presented with the help of molecular-dynamics simulations, is presented in a companion article in this issue.

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