Literature DB >> 16581843

Strength of multiple parallel biological bonds.

Todd Sulchek1, Raymond W Friddle, Aleksandr Noy.   

Abstract

Multivalent interactions play a critical role in a variety of biological processes on both molecular and cellular levels. We have used molecular force spectroscopy to investigate the strength of multiple parallel peptide-antibody bonds using a system that allowed us to determine the rupture forces and the number of ruptured bonds independently. In our experiments the interacting molecules were attached to the surfaces of the probe and sample of the atomic force microscope with flexible polymer tethers, and the unique mechanical signatures of the tethers determined the number of ruptured bonds. We show that the rupture forces increase with the number of interacting molecules and that the measured forces obey the predictions of a Markovian model for the strength of multiple parallel bonds. We also discuss the implications of our results to the interpretation of force spectroscopy measurements in multiple bond systems.

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Year:  2006        PMID: 16581843      PMCID: PMC1471875          DOI: 10.1529/biophysj.105.080291

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  20 in total

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9.  Dynamic force spectroscopy of parallel individual Mucin1-antibody bonds.

Authors:  Todd A Sulchek; Raymond W Friddle; Kevin Langry; Edmond Y Lau; Huguette Albrecht; Timothy V Ratto; Sally J DeNardo; Michael E Colvin; Aleksandr Noy
Journal:  Proc Natl Acad Sci U S A       Date:  2005-11-03       Impact factor: 11.205

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  22 in total

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3.  Effect of viscous drag on multiple receptor-ligand bonds rupture force.

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6.  Effects of multiple-bond ruptures on kinetic parameters extracted from force spectroscopy measurements: revisiting biotin-streptavidin interactions.

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8.  Multiple receptors involved in human rhinovirus attachment to live cells.

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9.  Rupture of multiple catch-slip bonds: Two-state two-pathway catch-slip bonds.

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Journal:  Eur Phys J E Soft Matter       Date:  2013-11-26       Impact factor: 1.890

10.  Estimating kinetic and thermodynamic parameters from single molecule enzyme-inhibitor interactions.

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