Please use this identifier to cite or link to this item:
|Title:||Single-molecular-level study of claudin-1-mediated adhesion||Authors:||Lim, T.S.
|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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Dec 7, 2019
WEB OF SCIENCETM
checked on Nov 28, 2019
checked on Nov 30, 2019
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.