Magnetic Tweezers-Based Force Clamp Reveals Mechanically Distinct apCAM Domain Interactions
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|Title:||Magnetic Tweezers-Based Force Clamp Reveals Mechanically Distinct apCAM Domain Interactions||Authors:||Kinlic, Devrim
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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