Single molecule force spectroscopy on ligand–DNA complexes: from molecular binding mechanisms to biosensor applications

Ros, Robert; Eckel, Rainer; Bartels, Frank Wilco; Sischka, Andy; Baumgarth, Birgit; Wilking, Sven David; Pühler, Alfred; Sewald, Norbert; Becker, Anke; Anselmetti, Dario

doi:10.1016/j.jbiotec.2004.04.029

Cited by 39 publications

(25 citation statements)

References 41 publications

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“…Due to the large number and the importance of the studies on ATP-dependent motors a whole section is devoted below to them. A large of number of studies have focused in the study of protein-protein interactions of the ligand-receptor type [238]. These interactions are governed by what in biological terms has become known as "lock and key" mechanism.…”

Section: Proteinsmentioning

confidence: 99%

Single-molecule experiments in biological physics: methods and applications

Ritort

2006

J. Phys.: Condens. Matter

389

463

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Abstract. I review single-molecule experiments (SME) in biological physics. Recent technological developments have provided the tools to design and build scientific instruments of high enough sensitivity and precision to manipulate and visualize individual molecules and measure microscopic forces. Using SME it is possible to: manipulate molecules one at a time and measure distributions describing molecular properties; characterize the kinetics of biomolecular reactions and; detect molecular intermediates. SME provide the additional information about thermodynamics and kinetics of biomolecular processes. This complements information obtained in traditional bulk assays. In SME it is also possible to measure small energies and detect large Brownian deviations in biomolecular reactions, thereby offering new methods and systems to scrutinize the basic foundations of statistical mechanics. This review is written at a very introductory level emphasizing the importance of SME to scientists interested in knowing the common playground of ideas and the interdisciplinary topics accessible by these techniques.

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Section: Proteinsmentioning

confidence: 99%

Single-molecule experiments in biological physics: methods and applications

Ritort

2006

J. Phys.: Condens. Matter

389

463

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“…Applying SMFS on the complexes, direct insights in the binding strength, transition states, energy landscape, and thermodynamic and kinetic parameters of many ligand‐receptor interactions or even cell mechanics can be detected. A detailed description of SMFS methodologies has been reviewed nicely …”

Section: Single‐molecule Force Spectroscopymentioning

confidence: 99%

“…A detailed description of SMFS methodologies has been reviewed nicely. 45,54,55 SMFS-based atomic force microscopy (AFS) in principle describes the force-displacement curves obtained by oscillating the scanner in z-direction, while the scanner movement in x-and y-directions is disabled. In such a way, the deflection signal from the cantilever and the movement of the piezoelectric scanner are recorded.…”

Section: Single-molecule Force Spectroscopymentioning

confidence: 99%

Single‐molecule force spectroscopy applied to heparin‐induced thrombocytopenia

Nguyen

2016

J of Molecular Recognition

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Heparin-induced thrombocytopenia (HIT), occurring up to approximately 1% to 5% of patients receiving the antithrombotic drug heparins, has a complex pathogenesis involving multiple partners ranging from small molecules to cells/platelets. Recently, insights into the mechanism of HIT have been achieved by using single-molecule force spectroscopy (SMFS), a methodology that allows direct measurements of interactions among HIT partners. Here, the potential of SMFS in unraveling the mechanism of the initial steps in the pathogenesis of HIT at single-molecule resolution is highlighted. The new findings ranging from the molecular binding strengths and kinetics to the determination of the boundary between risk and non-risk heparin drugs or platelet-surface and platelet-platelet interactions will be reviewed. These novel results together have contributed to elucidate the mechanisms underlying HIT and demonstrate how SMFS can be applied to develop safer drugs with a reduced risk profile.

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“…We have now modified the methodology of sample preparation and have adopted the socalled dynamic approach of the SMFS methodology. [24,[27][28][29] In fact, when a pulling force is applied to a folded protein, the dominant energy barrier that confines the folded structure is lowered. The most probable unfolding force therefore decreases with increasing applied force.…”

Section: Steered Molecular-dynamics Simulations Of the Angiostatin Mementioning

confidence: 99%

“…The dynamic approach of the SMFS methodology is based on the study of this dependence. [24,[27][28][29] This methodology makes it possible to locate the dominant barrier and estimate the folding lifetime extrapolated at zero force.…”

Section: Steered Molecular-dynamics Simulations Of the Angiostatin Mementioning

confidence: 99%

Hierarchical Mechanochemical Switches in Angiostatin

Grandi¹,

Sandal²,

Guarguaglini³

et al. 2006

ChemBioChem

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We wish to propose a novel mechanism by which the triggering of a biochemical signal can be controlled by the hierarchical coupling between a protein redox equilibrium and an external mechanical force. We have characterized this mechanochemical mechanism in angiostatin, and we have evidence that it can switch the access to partially unfolded structures of this protein. We have identified a metastable intermediate that is specifically accessible under thioredoxin-rich reducing conditions, like those met by angiostatin on the surface of a tumor cell. The structure of the same intermediate accounts for the unexplained antiangiogenic activity of angiostatin. These findings demonstrate a new link between redox biology and mechanically regulated processes.

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Single molecule force spectroscopy on ligand–DNA complexes: from molecular binding mechanisms to biosensor applications

Cited by 39 publications

References 41 publications

Single-molecule experiments in biological physics: methods and applications

Single-molecule experiments in biological physics: methods and applications

Single‐molecule force spectroscopy applied to heparin‐induced thrombocytopenia

Hierarchical Mechanochemical Switches in Angiostatin

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