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Related Experiment Videos

Non-covalent interactions between unsolvated peptides: helical complexes based on acid-base interactions.

Rajagopalan Sudha1, Motoya Kohtani, Martin F Jarrold

  • 1Chemistry Department, Indiana University, Bloomington, Indiana 47405-7102, USA.

The Journal of Physical Chemistry. B
|July 21, 2006
PubMed
Summary

We studied the structures of two helical peptides, AcA(7)KA(6)KK and AcEA(7)EA(7), using ion-mobility mass spectrometry. We found two conformations: a linear arrangement stabilized by a strong EKK interaction and a coiled-coil structure with a weaker hydrogen bond.

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Area of Science:

  • Biophysical Chemistry
  • Mass Spectrometry
  • Structural Biology

Background:

  • Helical peptides are fundamental in biological systems.
  • Understanding peptide complex conformations is crucial for drug design and biomaterials.
  • Designed interactions between acidic (glutamic acid, E) and basic (lysine, K) residues can stabilize peptide complexes.

Purpose of the Study:

  • To investigate the gas-phase conformations of protonated complexes formed between alanine-based helical peptides AcA(7)KA(6)KK and AcEA(7)EA(7).
  • To characterize the nature and strength of interactions stabilizing these peptide complexes.
  • To determine the thermodynamic parameters governing conformational changes.

Main Methods:

  • Ion-mobility mass spectrometry (IM-MS) was employed to analyze peptide complex structures in the gas phase.

Related Experiment Videos

  • Electrospray ionization was used to generate protonated peptide complexes.
  • Temperature-dependent measurements were performed to study conformational transitions.

    • Main Results:

    • Two distinct conformations were observed: a coaxial linear arrangement and a coiled-coil structure.
    • The linear conformation is stabilized by a strong glutamic acid-lysine-lysine (EKK) interaction.
    • The coiled-coil conformation, featuring a weaker glutamic acid-lysine (EK) hydrogen bond, opens to the linear form upon heating.

    Conclusions:

    • The study elucidates the conformational landscape of interacting helical peptides in the gas phase.
    • The findings highlight the role of specific residue interactions (EKK and EK) in stabilizing peptide complexes.
    • Thermodynamic analysis reveals the EK interaction to be a weak hydrogen bond, while the EKK interaction is significantly stronger.