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Peptides Derived from Angiogenin Regulate Cellular Copper Uptake.

Giovanni Tabbì1, Lorena Maria Cucci2, Calogero Pinzino3

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International Journal of Molecular Sciences
|September 10, 2021
PubMed
Summary
This summary is machine-generated.

The amino group in angiogenin (ANG) peptide fragments is key for copper binding and cellular uptake. Different copper complex geometries influence peptide activity, affecting intracellular copper levels differently.

Keywords:
angiogenesisconfocal microscopycopperelectron spin resonancemetal complexespeptidepotentiometryribonucleases

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Cell Biology

Background:

  • Angiogenin (ANG) is a potent endogenous angiogenic factor.
  • Copper ions play crucial roles in cellular processes.
  • Understanding metal-protein interactions is vital for biological insights.

Purpose of the Study:

  • To characterize copper complex species formed with N-terminal angiogenin peptide fragments (Ang1-17 and AcAng1-17).
  • To investigate the role of the amino group in copper binding and cellular uptake.
  • To compare the activity of peptide fragments with native (wtANG) and recombinant (rANG) angiogenin.

Main Methods:

  • Potentiometric, spectroscopic, and voltammetric techniques were used for complex characterization.
  • Confocal laser scanning microscopy analyzed cellular copper uptake in neuroblastoma cells.
  • Comparative analysis included wtANG and rANG.

Main Results:

  • The amino group is the primary copper anchoring site for Ang1-17.
  • Copper complex formation and redox potentials depend on copper equivalents added.
  • Free amino Ang1-17 enhances cellular copper uptake, while acetylated form decreases it.
  • wtANG increases intracellular copper, whereas rANG decreases it.

Conclusions:

  • Copper complex geometry significantly modulates peptide activity and cellular copper uptake.
  • The N-terminal amino group is critical for angiogenin peptide's interaction with copper.
  • Native wtANG influences cellular copper levels differently than recombinant rANG, highlighting the importance of protein form.