Force spectroscopy of LFA-1 and its ligands, ICAM-1 and ICAM-2

Ewa P. Wojcikiewicz, Midhat H. Abdulreda, Xiaohui Zhang, Vincent T. Moy

Research output: Contribution to journalArticlepeer-review

86 Scopus citations


Single-molecule measurements of the interaction of leukocyte function-associated antigen-1 (LFA-1), expressed on Jurkat T cells, with intercellular adhesion molecules-1 and -2 (ICAM-1 and ICAM-2) were conducted using atomic force microscopy (AFM). The force spectra (i.e., unbinding force versus loading rate) of both the LFA-1/ICAM-1 and LFA-1/ ICAM-2 interactions were acquired at a loading rate range covering 3 orders of magnitude (50-60 000 pN/s) and revealed a fast loading regime and a slow loading regime. This indicates that the dissociation of both complexes involves overcoming a steep inner and a wide outer activation barrier. LFA-1 binding to ICAM-I and ICAM-2 was strengthened in the slow loading regime by the addition of Mg2+. Differences in the dynamic strength of the LFA-1/ICAM-1 and LFA-1/ICAM-2 interactions can be attributed to the presence of wider barriers in the ICAM-2 complex, making it more responsive to a pulling force than the ICAM- I complex.

Original languageEnglish (US)
Pages (from-to)3188-3195
Number of pages8
Issue number11
StatePublished - Nov 2006

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry


Dive into the research topics of 'Force spectroscopy of LFA-1 and its ligands, ICAM-1 and ICAM-2'. Together they form a unique fingerprint.

Cite this