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Research Article Received: 2 April 2008 Revised: 5 August 2008 Accepted: 29 August 2008 Published online in Wiley Interscience: 26 November 2008
 

Summary: 5
Research Article
Received: 2 April 2008 Revised: 5 August 2008 Accepted: 29 August 2008 Published online in Wiley Interscience: 26 November 2008
(www.interscience.com) DOI 10.1002/psc.1078
Improving the interaction of Myc-interfering
peptides with Myc using molecular dynamics
simulations
Eva M. Jouaux,a Barbara B. Timm,a Katja M. Arndt,a,b,c and
Thomas E. Exnerd
Previously, a Myc-interfering peptide (Mip) was identified for the targeted inactivation of the Myc : Max complex by the
combination of rational design and an in vivo protein-fragment complementation assay. In the subsequent work presented
here, molecular dynamics simulations and free energy calculations based on the molecular mechanics GBSA method were
performed to define the contribution of the different amino acids in the Myc: Mip coiled coil domain, and compared to wild-type
Myc : Max. For further optimization of the Myc interference, point mutations were introduced into Mip and analyzed, from
which two showed much higher binding affinities in the computational studies in good agreement with the experiment. These
mutants with very high potential for inactivation of Myc can now be used as starting point for further optimizations based on
the computational as well as experimental protocols presented here. Copyright c 2008 European Peptide Society and John
Wiley & Sons, Ltd.
Keywords: oncogene; leucine zipper; bHLHZip motif; circular dichroism; free energy calculations
Introduction

  

Source: Arndt, Katja - Institut für Biologie III, Albert-Ludwigs-Universität Freiburg

 

Collections: Biotechnology; Biology and Medicine