Statistical Breakage of Single Protein A-IgG Bonds Reveals Crossover from Spontaneous to Force-Induced Bond Dissociation
- 19 July 1999
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 83 (3) , 652-655
- https://doi.org/10.1103/physrevlett.83.652
Abstract
Dynamic force spectroscopy was applied to single specific bonds between immunoglobulins of type G and protein A, a staphylococcal receptor for IgG. The resulting spectra of yield forces indicated the crossover from force induced to spontaneous bond dissociation. Moreover, failure of unloaded bonds was observed directly. Extrapolation to vanishing loading rate and direct observation yielded coinciding results.Keywords
This publication has 17 references indexed in Scilit:
- Micropipet-Based Pico Force Transducer: In Depth Analysis and Experimental VerificationBiophysical Journal, 1998
- Kinetics and locus of failure of receptor-ligand-mediated adhesion between latex spheres. I. Protein-carbohydrate bondBiophysical Journal, 1996
- Strength and lifetime of the bond between actin and skeletal muscle α-actinin studied with an optical trapping techniqueBiochimica et Biophysica Acta (BBA) - General Subjects, 1996
- Lifetime of the P-selectin-carbohydrate bond and its response to tensile force in hydrodynamic flowNature, 1995
- Transient intercellular adhesion: the importance of weak protein-protein interactionsTrends in Biochemical Sciences, 1994
- Adhesion Forces Between Individual Ligand-Receptor PairsScience, 1994
- Long-Range Attraction and Molecular Rearrangements in Receptor-Ligand InteractionsScience, 1992
- Force measurements by micromanipulation of a single actin filament by glass needlesNature, 1988
- Binding of immunoglobulins to protein A and immunoglobulin levels in mammalian seraJournal of Immunological Methods, 1983
- Models for the Specific Adhesion of Cells to CellsScience, 1978