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An alternative structure model for the polypentapeptide in elastin.

Peter C Gross¹, Wulff Possart, Michael Zeppezauer

¹Fraunhofer-Institute for Manufacturing and Applied Materials Research (IFAM), Wiener Strasse 12, D-28359 Bremen, Germany.

Zeitschrift Fur Naturforschung. C, Journal of Biosciences

|January 10, 2004

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Polypentapeptide (PPP) films convert energy to mechanical work via a deltaT(t)-mechanism. This study finds the beta-sheet, not the beta-spiral, is the key conformation in PPP elasticity.

Area of Science:

Biomaterials Science
Polymer Chemistry
Biophysics

Background:

Polypentapeptides (PPP) mimic elastin, a connective tissue protein.
The deltaT(t)-mechanism in PPP films converts energy to mechanical work.
A beta-spiral conformation was previously proposed to explain this mechanism.

Purpose of the Study:

To investigate the secondary structure of linear polypentapeptide C(GVGVP)6 in solution.
To determine the conformational basis of the deltaT(t)-mechanism in polypentapeptides.
To re-evaluate the proposed beta-spiral model for polypentapeptide conformation.

Main Methods:

Differential Scanning Calorimetry (DSC)
Circular Dichroism (CD) spectroscopy
UV-Visible absorption spectroscopy

Related Experiment Videos

Fourier-Transform Infrared (FTIR) spectroscopy

Nuclear Magnetic Resonance (NMR) spectroscopy

Main Results:

Spectroscopic data did not support the presence of a beta-spiral conformation in polypentapeptides.
An antiparallel beta-sheet structure was found to be consistent with all experimental data.
This suggests a revised understanding of polypentapeptide conformational dynamics.

Conclusions:

The beta-spiral model for polypentapeptide conformation is likely incorrect.
The antiparallel beta-sheet is proposed as the fundamental regular conformation.
This finding necessitates a new perspective on the elasticity of natural elastin and synthetic polypentapeptides.