An alternative structure model for the polypentapeptide in elastin
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Updated: Aug 29, 2026

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
Published on: June 9, 2014
Peter C Gross1, Wulff Possart, Michael Zeppezauer
1Fraunhofer-Institute for Manufacturing and Applied Materials Research (IFAM), Wiener Strasse 12, D-28359 Bremen, Germany.
Abstract:
Polypentapeptides (GVGVP)n which are designed in analogy to the connective tissue protein elastin are reported to transform various kinds of energy into mechanical work by the so-called deltaT(t)-mechanism in cross-linked macroscopic polypentapeptide (PPP) films. In the literature, the responsible element of conformation in such polypeptides is described as a beta-spiral and the deltaT(t) effect is explained as a sudden change of macroconformation of single polypeptide molecules from an extended but not regular state below a transition temperature T(t) to the beta-spiral above T(t). We examined the secondary structure of the linear PPP C(GVGVP)6 in solution with DSC, CD, UV absorption, FTIR and NMR spectroscopy. The results suggest that the beta-spiral is not present in the conformational structure of the PPP molecules. The antiparallel beta-sheet is proposed to be the basic regular part of conformation because it agrees with all spectroscopic data. As a consequence, the elasticity of natural elastin must be considered from a new perspective.
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