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pH dependent conformation of physalaemin.

G Hölzemann1, K G Pachler

  • 1Medicinal Chemistry Department, E. Merck, Darmstadt, Federal Republic of Germany.

International Journal of Peptide and Protein Research
|August 1, 1989
PubMed
Summary

Nuclear magnetic resonance (NMR) revealed physalaemin adopts a flexible structure in acidic conditions but folds into a beta turn at neutral pH. This conformational change is driven by charged amino acids Asp and Lys.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Spectroscopy

Background:

  • Physalaemin is an undecapeptide with known biological activities.
  • Understanding peptide conformation is crucial for structure-activity relationship studies.

Purpose of the Study:

  • To elucidate the solution structure of physalaemin under varying pH conditions using NMR spectroscopy.
  • To investigate the conformational changes influenced by pH and charged residues.

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy was employed.
  • Experiments were conducted in DMSO solution at acidic (pH 3.5) and neutral (pH 7.0) conditions.

Main Results:

  • Significant changes in NH chemical shifts and proton temperature gradients were observed between pH 3.5 and 7.0, particularly for Asp and Lys residues.
  • At pH 3.5, physalaemin exhibited a flexible conformation.
  • At neutral pH, a folded structure emerged, characterized by two interresidue and one intraresidue hydrogen bond, including a beta turn involving proline and asparagine.

Conclusions:

  • Physalaemin undergoes a pH-dependent conformational transition from a flexible to a folded state.
  • The charged residues Asp and Lys play a key role in mediating this structural change.
  • The folded structure at neutral pH features a specific beta turn, influencing peptide conformation.

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