Energy Landscape of Streptavidin−Biotin Complexes Measured by Atomic Force Microscopy

Yuan, Changxia; Chen, Aileen B.; Kolb, Pamela; Moy, Vincent T.

doi:10.1021/bi992715o

Cited by 266 publications

(283 citation statements)

References 30 publications

(50 reference statements)

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“…The presence of more than one linear regime indicates the existence of several energy barriers. (See also [1135][1136][1137].) The same dependence on the loading rate has been found also for DNA [1138].…”

Section: Rupture Force Of Specific Interactionssupporting

confidence: 64%

Force measurements with the atomic force microscope: Technique, interpretation and applications

Butt

Cappella

Kappl

2005

Surface Science Reports

3,204

2,949

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Section: Rupture Force Of Specific Interactionssupporting

confidence: 64%

Force measurements with the atomic force microscope: Technique, interpretation and applications

Butt

Cappella

Kappl

2005

Surface Science Reports

3,204

2,949

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“…the rate at which force builds up on the respective bonds). Loading rates (pN/second) were computed as the product of the slope of the force-distance curve (pN/nm) just before a rupture event -the effective force constant that takes the viscoelastic properties of the system into account (Evans and Ritchie, 1999;Yuan et al, 2000) -and the pulling velocity (nm/second). Pulling velocities were varied from 250-12,500 nm/second.…”

Section: Rupture-force Measurements and Force Spectroscopymentioning

confidence: 99%

Distinct kinetic and mechanical properties govern ALCAM-mediated interactions as shown by single-molecule force spectroscopy

Riet

Zimmerman

Cambi

et al. 2007

Journal of Cell Science

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The activated leukocyte cell adhesion molecule (ALCAM) mediates dynamic homotypic and heterotypic cellular interactions. Whereas homotypic ALCAM-ALCAM interactions have been implicated in the development and maintenance of tissue architecture and tumor progression, heterotypic ALCAM-CD6 interactions act to initiate and stabilize T-cell–dendritic-cell interactions affecting T-cell activation. The ability to resist the forces acting on the individual bonds during these highly dynamic cellular contacts is thought to be crucial for the (patho)physiology of ALCAM-mediated cell adhesion. Here, we used atomic force microscopy to characterize the relationship between affinity, avidity and the stability of ALCAM-mediated interactions under external loading, at the single-molecule level. Disruption of the actin cytoskeleton resulted in enhanced ALCAM binding avidity, without affecting the tensile strength of the individual bonds. Force spectroscopy revealed that the ALCAM-CD6 bond displayed a significantly higher tensile strength, a smaller reactive compliance and an up to 100-fold lower dissociation rate in the physiological force window in comparison to the homotypic interaction. These results indicate that homotypic and heterotypic ALCAM-mediated adhesion are governed by significantly distinct kinetic and mechanical properties, providing novel insight into the role of ALCAM during highly dynamic cellular interactions.

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“…where r represents the loading rate of the bond (7,16). The Bell model thus predicts a linear relationship between the logarithm of loading rate and rupture force of the single bond.…”

Section: Modelmentioning

confidence: 99%

“…A tomic force microscopy (1-4) and force spectroscopy (5,6) have been used to reveal the properties of the weak noncovalent bond between receptor molecules and their ligands, and in particular dynamic force spectroscopy has been used to define in detail the properties of the single biotin-avidin bond (1)(2)(3)7). As regarding molecular motors, the optical tweezers technique has allowed the investigation of the properties of an individual actomyosin bond and to measure the force and unitary step displacement generated (8)(9)(10).…”

mentioning

confidence: 99%

Characterization of actomyosin bond properties in intact skeletal muscle by force spectroscopy

Colombini

Bagni

Romano

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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Force generation and motion in skeletal muscle result from interaction between actin and myosin myofilaments through the cyclical formation and rupture of the actomyosin bonds, the crossbridges, in the overlap region of the sarcomeres. Actomyosin bond properties were investigated here in single intact muscle fibers by using dynamic force spectroscopy. The force needed to forcibly detach the cross-bridge ensemble in the half-sarcomere (hs) was measured in a range of stretching velocity between 3.4 ؋ 10 3 nm⅐hs ؊1 ⅐s ؊1 or 3.3 fiber length per second (l0s ؊1 ) and 6. cross-bridges ͉ rupture force ͉ detachment rate constant ͉ fast stretches A tomic force microscopy (1-4) and force spectroscopy (5, 6) have been used to reveal the properties of the weak noncovalent bond between receptor molecules and their ligands, and in particular dynamic force spectroscopy has been used to define in detail the properties of the single biotin-avidin bond (1-3, 7). As regarding molecular motors, the optical tweezers technique has allowed the investigation of the properties of an individual actomyosin bond and to measure the force and unitary step displacement generated (8-10). The properties of the single actomyosin bond under rigor conditions were also investigated by measuring the dependence of the bond lifetime on the applied load (11). It was found that bond lifetime was strongly reduced when a load was applied to the bond, in good quantitative agreement with the prediction of Bell theory (12). These results on single actomyosin interaction represent a great step forward in our understanding of molecular mechanism of force generation in muscle; however, they were generally obtained under experimental conditions that differ from those encountered by the same motors in native preparation. In living skeletal muscle, myosin heads (the molecular motors) are distributed over the myosin filament in a very regular fashion, and both actin and myosin filaments are arranged in a quasicrystalline lattice that maintains a precise geometrical relationship between myosin heads (or fraction S1 of myosin molecule) and the active sites regularly distributed along the actin filament (13). This remarkable order is lost when experiments are made on single molecules, and this may affect the bond properties and force developed. In addition, at physiological ionic strength, actin filaments tend to detach from myosin heads, and it is therefore necessary to perform the above experiments at low ionic strength. However, it is known that molecular motor performance strongly depends on ionic strength (14). The force generated is also strongly affected by myosin S1 orientation, which is not easily controlled in single-molecule experiments (14). This means that the force measured by the recording apparatus, usually along the actin filament axis, may not represent accurately the real capability of the motors when working in a regularly ordered array. The same is true in experiments in which an external load is applied to the single bond, because it is usually d...

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Energy Landscape of Streptavidin−Biotin Complexes Measured by Atomic Force Microscopy

Cited by 266 publications

References 30 publications

Force measurements with the atomic force microscope: Technique, interpretation and applications

Force measurements with the atomic force microscope: Technique, interpretation and applications

Distinct kinetic and mechanical properties govern ALCAM-mediated interactions as shown by single-molecule force spectroscopy

Characterization of actomyosin bond properties in intact skeletal muscle by force spectroscopy

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