Nectins are Ca2+ independent cell adhesion molecules localizing at the cadherin based adherens junctions. In this study, we have used atomic force microscopy to study interaction of a chimera of extra cellular fragment of nectin-1 and Fc of human IgG (nef-1) with wild type L-fibroblasts that express endogenous nectin-1 to elucidate the biophysical characteristics of homophilic nectin-1 traps-interactions at the level of single molecule. Bond strength distribution revealed three distinct bound states (or configurations) of traps-interactions between paired nectins, where each bound state has a unique unstressed off-rate and reactive compliance. Kinetic analysis of force-dependent off-rate of the bound state involving traps-interacting V-V domains between paired nectin-1 (unstressed off-rate similar to 1.465 +/- 0.779 s(-1), reactive compliance similar to 0.143 +/- 0.072 nm) was found to be closest to E-cadherin, indicating that V-V domain traps-interactions are probably necessary to initiate and promote adhesions of E-cadherin at adherens junctions (AJs). (c) 2007 Elsevier Inc. All rights reserved.