Bihr T, Fenz S, Sackmann E, Merkel R, Seifert U, Sengupta K, Smith AS (2014)
Publication Language: English
Publication Status: Published
Publication Type: Journal article, Original article
Publication year: 2014
Publisher: CELL PRESS
Book Volume: 107
Pages Range: L33-L36
Journal Issue: 11
URI: http://www.sciencedirect.com/science/article/pii/S0006349514011163
DOI: 10.1016/j.bpj.2014.10.033
Thus far, understanding how the confined cellular environment affects the lifetime of bonds, as well as the extraction of complexation rates, has been a major challenge in studies of cell adhesion. Based on a theoretical description of the growth curves of adhesion domains, we present a new (to our knowledge) method to measure the association rate k(on) of ligand-receptor pairs incorporated into lipid membranes. As a proof of principle, we apply this method to several systems. We find that the k(on) for the interaction of biotin with neutravidin is larger than that for integrin binding to RGD or sialyl Lewis(x) to E-selectin. Furthermore, we find k(on) to be enhanced by membrane fluctuations that increase the probability for encounters between the binders. The opposite effect on k(on) could be attributed to the presence of repulsive polymers that mimic the glycocalyx, which points to two potential mechanisms for controlling the speed of protein complexation during the cell recognition process.
APA:
Bihr, T., Fenz, S., Sackmann, E., Merkel, R., Seifert, U., Sengupta, K., & Smith, A.-S. (2014). Association Rates of Membrane-Coupled Cell Adhesion Molecules. Biophysical Journal, 107(11), L33-L36. https://doi.org/10.1016/j.bpj.2014.10.033
MLA:
Bihr, Timo, et al. "Association Rates of Membrane-Coupled Cell Adhesion Molecules." Biophysical Journal 107.11 (2014): L33-L36.
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