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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Force-induced prolyl cis-trans isomerization in elastin-like polypeptides.

Alexei Valiaev¹, Dong Woo Lim, Terrence G Oas

¹Department of Mechanical Engineering and Materials Science, and Center for Biologically Inspired Materials and Materials Systems, Duke University, Durham, NC 27708, USA.

Journal of the American Chemical Society

|May 2, 2007

Summary

Single-molecule force spectroscopy revealed that elastin-like polypeptides (ELPs) undergo temperature-independent elongation due to force-induced prolyl cis-trans isomerization. This finding offers a new method for studying this key conformational change in polypeptides.

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Area of Science:

Biophysics
Polymer Science
Structural Biology

Background:

Elastin-like polypeptides (ELPs) are stimulus-responsive polymers with repeating VPGXG sequences.
Conformational mechanics of ELPs are typically studied under various solvent conditions.

Purpose of the Study:

To investigate unexplained extensional transitions observed in ELP force-extension curves.
To identify the molecular mechanism behind force-induced conformational changes in ELPs.

Main Methods:

Single-molecule force spectroscopy (SMFS) to measure force-extension curves.
Control experiments using poly(L-proline) and poly(L-lysine).
Monte Carlo simulations using an elastically coupled, two-state model.

Main Results:

Observed temperature-independent extensional transitions in ELPs not explained by standard polymer models.
Identified force-induced peptidyl-prolyl cis-trans isomerization as the cause of elongation.
Demonstrated similar transitions in poly(L-proline) but not poly(L-lysine).
Hysteresis experiments suggested exhaustion of the cis proline state.

Conclusions:

Force-induced prolyl cis-trans isomerization is a key mechanism in ELP conformational changes.
SMFS can be utilized to assay prolyl cis-trans isomerization in polypeptides.
This study provides the first demonstration of force-induced prolyl cis-trans isomerization in proline-containing polypeptides.