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The dynamics of interleukin-8 and its interaction with human CXC receptor I peptide

Agnieszka A Kendrick1, Michael J Holliday, Nancy G Isern

  • 1Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Denver, Aurora, Colorado, 80224.

Protein Science : a Publication of the Protein Society
|January 21, 2014
PubMed

Insights

Interleukin-8 (CXCL8) monomers bind its receptor (CXCR1) with higher affinity than dimers. This study clarifies CXCL8

Area of Science:

  • Immunology
  • Biochemistry
  • Molecular Biology

Background:

  • Interleukin-8 (CXCL8) is a key proinflammatory chemokine regulating immune responses.
  • CXCL8 interacts with G-protein coupled receptors like CXC receptor 1 (CXCR1).
  • The roles of CXCL8 monomer and dimer in receptor binding are poorly understood, with conflicting biophysical data.

Purpose of the Study:

  • To elucidate the molecular basis of CXCL8 monomer and dimer binding to CXCR1.
  • To resolve conflicting biophysical findings on CXCL8-CXCR1 interactions.
  • To investigate the binding dynamics of wild-type CXCL8 and a monomer-stabilizing mutant (CXCL8M).

Main Methods:

  • Peptide corresponding to the N-terminal region of human CXCR1 (hCXCR1pep) was expressed and purified.
  • Nuclear magnetic resonance (NMR) spectroscopy was employed to study binding interactions.
  • Binding affinities of CXCL8 monomer and dimer to hCXCR1pep were compared.

Main Results:

  • The CXCL8 monomer demonstrated slightly higher binding affinity to hCXCR1pep compared to the CXCL8 dimer.
  • CXCL8 dimers did not dissociate upon binding to hCXCR1pep.
  • CXCL8 exhibits dynamic behavior across multiple timescales, potentially influencing receptor engagement.

Conclusions:

  • CXCL8 monomer binding to CXCR1 is favored over dimer binding.
  • CXCL8 dimer stability is maintained during receptor interaction.
  • The dynamic nature of CXCL8 contributes to its versatile receptor interactions.

Keywords:
NMRdimerdynamicshuman CXC receptor 1interleukin-8

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