Please use this identifier to cite or link to this item: https://doi.org/10.1021/la702436x
Title: Single-molecular-level study of claudin-1-mediated adhesion
Authors: Lim, T.S.
Vedula, S.R.K. 
Kausalya, P.J.
Hunziker, W.
Lim, C.T. 
Issue Date: 15-Jan-2008
Citation: Lim, T.S., Vedula, S.R.K., Kausalya, P.J., Hunziker, W., Lim, C.T. (2008-01-15). Single-molecular-level study of claudin-1-mediated adhesion. Langmuir 24 (2) : 490-495. ScholarBank@NUS Repository. https://doi.org/10.1021/la702436x
Abstract: Claudins are proteins that are selectively expressed at tight junctions (TJs) of epithelial cells where they play a central role in regulating paracellular permeability of solutes across epithelia. However, the role of claudins in intercellular adhesion and the mechanism by which they regulate the diffusion of solutes are poorly understood. Here, using single molecule force spectroscopy, the kinetic properties and adhesion strength of homophilic claudin-1 interactions were probed at the single-molecule level. Within the range of tested loading rates (103-105 pN/s), our results showed that homophilic claudin-1 interactions have a reactive compliance of 0.363 ±0.061 nm and an unstressed dissociation rate of 1.351 ±1.312 s-1. This is more than 100-fold greater than that of E-cadherin. The weak and short-lived interactions between claudin-1 molecules make them highly unstable and dynamic in nature. Such a dynamic interaction is consistent with a model where breaking and resealing of TJ strands regulate the paracellular diffusion of solutes. © 2008 American Chemical Society.
Source Title: Langmuir
URI: http://scholarbank.nus.edu.sg/handle/10635/85639
ISSN: 07437463
DOI: 10.1021/la702436x
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