Analysis of Selected and Designed Chimeric D- and L-alpha-Helix Assemblies

Kuekenshoener T, Hagemann UB, Wohlwend D, Raeuber C, Baumann T, Keller S, Einsle O, Müller K, Arndt KM (2014)
Biomacromolecules 15(9): 3296-3305.

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Abstract
D-Peptides have been attributed pharmacological advantages over regular L-peptides, yet design rules are largely unknown. Based on a designed coiled coil-like D/L heterotetramer, named L-Base/D-Acid, we generated a library offering alternative residues for interaction with the D-peptide. Phage display selection yielded one predominant peptide, named HelixA, that differed at 13 positions from the scaffold helix. In addition to the observed D-/L-heterotetramers, ratio-dependent intermediate states were detected by isothermal titration calorimetry. Importantly, the formation of the selected HelixA/D-Acid bundle passes through fewer intermediate states than L-Base/D-Acid. Back mutation of HelixA core residues to L-Base (HelixLL) revealed that the residues at e/g-positions are responsible for the different intermediates. Furthermore, a Val-core variant (PeptideVV) was completely devoid of binding D-Acid, whereas an Ile-core helix (HelixII) interacted with D-Acid in a significantly more specific complex than L-Base.
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Kuekenshoener T, Hagemann UB, Wohlwend D, et al. Analysis of Selected and Designed Chimeric D- and L-alpha-Helix Assemblies. Biomacromolecules. 2014;15(9):3296-3305.
Kuekenshoener, T., Hagemann, U. B., Wohlwend, D., Raeuber, C., Baumann, T., Keller, S., Einsle, O., et al. (2014). Analysis of Selected and Designed Chimeric D- and L-alpha-Helix Assemblies. Biomacromolecules, 15(9), 3296-3305.
Kuekenshoener, T., Hagemann, U. B., Wohlwend, D., Raeuber, C., Baumann, T., Keller, S., Einsle, O., Müller, K., and Arndt, K. M. (2014). Analysis of Selected and Designed Chimeric D- and L-alpha-Helix Assemblies. Biomacromolecules 15, 3296-3305.
Kuekenshoener, T., et al., 2014. Analysis of Selected and Designed Chimeric D- and L-alpha-Helix Assemblies. Biomacromolecules, 15(9), p 3296-3305.
T. Kuekenshoener, et al., “Analysis of Selected and Designed Chimeric D- and L-alpha-Helix Assemblies”, Biomacromolecules, vol. 15, 2014, pp. 3296-3305.
Kuekenshoener, T., Hagemann, U.B., Wohlwend, D., Raeuber, C., Baumann, T., Keller, S., Einsle, O., Müller, K., Arndt, K.M.: Analysis of Selected and Designed Chimeric D- and L-alpha-Helix Assemblies. Biomacromolecules. 15, 3296-3305 (2014).
Kuekenshoener, Tim, Hagemann, Urs B., Wohlwend, Daniel, Raeuber, Christina, Baumann, Tobias, Keller, Sandro, Einsle, Oliver, Müller, Kristian, and Arndt, Katja M. “Analysis of Selected and Designed Chimeric D- and L-alpha-Helix Assemblies”. Biomacromolecules 15.9 (2014): 3296-3305.
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