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Penultimate proline in neuropeptides.

Matthew S Glover1, Earl P Bellinger1, Predrag Radivojac1

  • 1†Department of Chemistry, ‡Department of Computer Science and Informatics, Indiana University, Bloomington, Indiana 47405, United States.

Analytical Chemistry
|July 21, 2015
PubMed
Summary
This summary is machine-generated.

Penultimate proline residues in neuropeptides enable multiple conformations through cis-trans isomerization. This conformational heterogeneity, revealed by ion mobility spectrometry-mass spectrometry (IMS-MS), offers a new perspective beyond enzymatic protection.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Proteomics

Background:

  • Tryptic peptide ions with a penultimate proline (Proline at the second position from the N-terminus) exhibit multiple conformations.
  • This conformational flexibility is attributed to the cis-trans isomerization of the Xaa(1)-Pro(2) peptide bond.
  • Penultimate proline residues are prevalent in neuropeptides.

Purpose of the Study:

  • To statistically analyze the frequency of penultimate proline residues in neuropeptides.
  • To investigate the impact of penultimate proline on neuropeptide conformations using ion mobility spectrometry-mass spectrometry (IMS-MS).
  • To explore the role of penultimate proline in neuropeptide structure and function.

Main Methods:

  • Statistical analysis of a neuropeptide database.
  • Ion mobility spectrometry-mass spectrometry (IMS-MS) experiments.
  • Conformational analysis of model neuropeptides, including N-terminal human neuropeptide Y (NPY1-9) and CabTRP Ia.

Main Results:

  • Penultimate proline residues are frequently observed in neuropeptides.
  • IMS-MS experiments confirmed that penultimate prolines facilitate the population of multiple conformations.
  • These conformations arise from the cis-trans isomerization of the Xaa(1)-Pro(2) peptide bond.
  • The study identified conformational heterogeneity as a significant role of penultimate prolines.

Conclusions:

  • Penultimate proline residues contribute significantly to the conformational diversity of neuropeptides.
  • Beyond potential roles in enzymatic degradation, penultimate prolines enhance neuropeptide structural flexibility.
  • This conformational heterogeneity may be crucial for neuropeptide biological activity and function.