Membrane interaction of the N-terminal domain of chemokine receptor CXCR1

Sourav Haldar, H. Raghuraman, Trishool Namani, Krishna Rajarathnam, Amitabha Chattopadhyay

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


The N-terminal domain of chemokine receptors constitutes one of the two critical ligand binding sites, and plays important roles by mediating binding affinity, receptor selectivity, and regulating function. In this work, we monitored the organization and dynamics of a 34-mer peptide of the CXC chemokine receptor 1 (CXCR1) N-terminal domain and its interaction with membranes by utilizing a combination of fluorescence-based approaches and surface pressure measurements. Our results show that the CXCR1 N-domain 34-mer peptide binds vesicles of 1,2-dioleoyl-. sn-glycero-3-phosphocholine (DOPC) and upon binding, the tryptophan residues of the peptide experience motional restriction and exhibit red edge excitation shift (REES) of 19. nm. These results are further supported by increase in fluorescence anisotropy and mean fluorescence lifetime upon membrane binding. These results constitute one of the first reports demonstrating membrane interaction of the N-terminal domain of CXCR1 and gain relevance in the context of the emerging role of cellular membranes in chemokine signaling.

Original languageEnglish (US)
Pages (from-to)1056-1061
Number of pages6
JournalBiochimica et Biophysica Acta - Biomembranes
Issue number6
StatePublished - Jun 2010
Externally publishedYes


  • Chemokine receptor
  • G-protein coupled receptor
  • Lipid monolayer
  • Membrane vesicle
  • Red edge excitation shift
  • Surface pressure

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


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