Magnetic Tweezers-Based Force Clamp Reveals Mechanically Distinct apCAM Domain Interactions

Title: Magnetic Tweezers-Based Force Clamp Reveals Mechanically Distinct apCAM Domain Interactions
Authors: Kinlic, Devrim
Blasiak, Agata
O'Mahony, James
Suter, Daniel M.
Lee, Gil U.
Permanent link: http://hdl.handle.net/10197/8451
Date: 19-Sep-2012
Abstract: Cell adhesion molecules of the immunoglobulin superfamily (IgCAMs) play a crucial role in cell-cell interactions during nervous system development and function. The Aplysia CAM (apCAM), an invertebrate IgCAM, shares structural and functional similarities with vertebrate NCAM and therefore has been considered as the Aplysia homolog of NCAM. Despite these similarities, the binding properties of apCAM have not been investigated thus far. Using magnetic tweezers, we applied physiologically relevant, constant forces to apCAM-coated magnetic particles interacting with apCAM-coated model surfaces and characterized the kinetics of bond rupture. The average bond lifetime decreased with increasing external force, as predicted by theoretical considerations. Mathematical simulations suggest that the apCAM homophilic interaction is mediated by two distinct bonds, one involving all five immunoglobulin (Ig)-like domains in an antiparallel alignment and the other involving only two Ig domains. In summary, this study provides biophysical evidence that apCAM undergoes homophilic interactions, and that magnetic tweezers-based, force-clamp measurements provide a rapid and reliable method for characterizing relatively weak CAM interactions.
Funding Details: European Commission
Science Foundation Ireland
Type of material: Journal Article
Publisher: Biophysical Society
Copyright (published version): 2012 Biophysical Society
Keywords: Cell adhesion molecule;Aplysia;Magnetic tweezers;Force differentiation assay;Mathematical modelling
DOI: 10.1016/j.bpj.2012.08.025
Language: en
Status of Item: Peer reviewed
Appears in Collections:Conway Institute Research Collection
Medicine Research Collection
Chemistry Research Collection

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