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Structural and Spectroscopic Characterization of a Histidine-Containing Tetrapeptide Crystallized with Copper

Yumie Nishiyama1, Vanessa Seudo Dimo1, Kazunori Motai1

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Metal coordination influences peptide crystallization. Copper ions alter histidine-containing tetrapeptide crystal structure and morphology, demonstrating metal-peptide interactions

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Area of Science:

  • Biophysical Chemistry
  • Materials Science
  • Crystallography

Background:

  • Metal coordination is a key strategy for controlling peptide self-assembly.
  • Understanding metal-peptide interactions is crucial for designing stable peptide crystals.

Purpose of the Study:

  • To investigate the effect of copper ions on the crystallization of a histidine-containing tetrapeptide.
  • To elucidate the role of metal coordination in modulating peptide assembly and crystal architecture.

Main Methods:

  • Single-crystal X-ray diffraction (sc-XRD) for structural analysis.
  • Angle-resolved polarized Raman spectroscopy to probe metal-peptide coordination.
  • Crystallization experiments in the presence and absence of copper ions.

Main Results:

  • Copper-free crystals showed rod-like morphology stabilized by hydrogen bonding.
  • Copper-containing crystals exhibited needle-like morphology with altered molecular orientation.
  • Raman spectroscopy confirmed copper coordination with histidine side chains, indicating modulated intermolecular packing.

Conclusions:

  • Metal coordination significantly influences peptide crystallization behavior and crystal architecture.
  • Copper-ion binding alters the self-assembly of histidine-containing tetrapeptides.
  • Vibrational spectroscopy is effective for studying metal-peptide interactions in crystalline structures.