In situ observation of streptavidin‐biotin binding on an immunoassay well surface using an atomic force microscope

Allen, Stephanie; Davies, John A.; Dawkes, Adrian; Davies, Martyn C.; Edwards, John C.; Parker, Marie Claire; Roberts, Clive J.; Sefton, J.; Tendler, Saul J. B.; Williams, Philip M.

doi:10.1016/0014-5793(96)00651-5

Cited by 73 publications

(47 citation statements)

References 24 publications

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“…The same kind of measurements have been performed by Allen et al [193]. No adhesion is observed when the streptavidin is blocked, and the specific force tums out to be 409 + 166 pN.…”

Section: Specific Forcessupporting

confidence: 53%

Force-distance curves by atomic force microscopy

Cappella

Dietler

1999

Surface Science Reports

1,486

1,025

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“…The same kind of measurements have been performed by Allen et al [193]. No adhesion is observed when the streptavidin is blocked, and the specific force tums out to be 409 + 166 pN.…”

Section: Specific Forcessupporting

confidence: 53%

Force-distance curves by atomic force microscopy

Cappella

Dietler

1999

Surface Science Reports

1,486

1,025

View full text Add to dashboard Cite

“…Although the single-bond forces derived from Poisson analysis are widely interpreted as hydrogen bonds (5,8,26,27), the typical rupture forces of a hydrogen bond are reportedly about 0.01 nN (19,20), orders of magnitude smaller than the f SR values in Table 1. On the other hand, ligand-receptor bonds, e.g., the streptavidin-biotin interaction, are reported to be on the order of 0.1 nN (4,16,24,25), which is comparable to the f SR values in Table 1 and suggests that multiple hydrogen bonds are involved in one ligand-receptor bond. Indeed, X-ray crystallography has proven that multiple hydrogen bonds are involved in ligand-receptor bonds (40).…”

Section: Poisson Analysis Of Bacterial Adhesion Forcessupporting

confidence: 52%

Statistical Analysis of Long- and Short-Range Forces Involved in Bacterial Adhesion to Substratum Surfaces as Measured Using Atomic Force Microscopy

Chen

Busscher

Mei

et al. 2011

Appl Environ Microbiol

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Surface thermodynamic analyses of microbial adhesion using measured contact angles on solid substrata and microbial cell surfaces are widely employed to determine the nature of the adhesion forces, i.e., the interplay between Lifshitz-van der Waals and acid-base forces. While surface thermodynamic analyses are often viewed critically, atomic force microscopy (AFM) can also provide information on the nature of the adhesion forces by means of Poisson analysis of the measured forces. This review first presents a description of Poisson analysis and its underlying assumptions. The data available from the literature for different combinations of bacterial strains and substrata are then summarized, leading to the conclusion that bacterial adhesion to surfaces is generally dominated by short-range, attractive acid-base interactions, in combination with long-range, weaker Lifshitz-van der Waals forces. This is in line with the findings of surface thermodynamic analyses of bacterial adhesion. Comparison with single-molecule ligand-receptor forces from the literature suggests that the short-range-force contribution from Poisson analysis involves a discrete adhesive bacterial cell surface site rather than a single molecular force. The adhesion force arising from these cell surface sites and the number of sites available may differ from strain to strain. Force spectroscopy, however, involves the tedious task of identifying the minor peaks in the AFM retraction force-distance curve. This step can be avoided by carrying out Poisson analysis on the work of adhesion, which can also be derived from retraction force-distance curves. This newly proposed way of performing Poisson analysis confirms that multiple molecular bonds, rather than a single molecular bond, contribute to a discrete adhesive bacterial cell surface site.Bacteria can adhere to various natural (33) and synthetic (11) surfaces, a phenomenon with widely different fields of application ranging from marine fouling, soil remediation, and food and drinking water processing to medicine and dentistry. In order to avoid the problems sometimes associated with bacterial adhesion, or to take advantage of it, better understanding of the mechanisms by which bacteria adhere to surfaces is required.Bacterial adhesion to surfaces can be approached by biochemical methods, by which the molecular structures mediating adhesion are unraveled (5, 18, 22, 31), or by physicochemical methods. Surface thermodynamic analyses of bacterial cell and substratum surfaces using measured contact angles with liquids have not only indicated when thermodynamic conditions are favorable or unfavorable for adhesion (1, 37) but can also be employed in combination with measured zeta potentials of the interacting surfaces to determine the nature of the adhesion forces that mediate initial adhesion, i.e., the interplay among long-range (Lifshitz-van der Waals [LW] and electrical double-layer [EDL]) and short-range (Lewis acid-base [AB]) interaction forces (35). Surface thermodynamic analyses of bacterial ad...

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“…The high specificity and affinity [46] of the complex, and the availability of structural and thermodynamic data made it an ideal model system. The reported unbinding forces for the streptavidin-biotin complex, however, were found to vary considerably, yielding force estimates from 83 to 410 pN [26][27][28]47]. Such deviations in rupture force have since been attributed to variances in the rate at which the biomolecular bond was loaded.…”

Section: Investigations Of Intermolecular Interactionsmentioning

confidence: 81%

Measuring and visualizing single molecular interactions in biology

Allen

Rigby-Singleton

Harris

et al. 2003

Biochemical Society Transactions

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In recent years, considerable attention has focused upon the biological applications of the atomic force microscope (AFM), and in particular in its ability to explore biomolecular interaction events at the single molecule level. Such measurements can provide considerable advantages, as they remove the data averaging inherent in other biophysical/biochemical approaches that record measurements over large ensembles of molecules. To this end AFM has been used for both the high-resolution imaging of a range of individual biological molecules and their complexes, and to record interaction forces between single interacting molecules. In a recently initiated project we have begun to utilize these approaches to explore the interactions of a range of biologically important peptides with model and cell membrane surfaces. In this review, the potential value of AFM for the investigation of a range of biomolecular interaction events will be discussed, but highlighting in particular its potential for the study of interactions of peptides/proteins with biological membranes.

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In situ observation of streptavidin‐biotin binding on an immunoassay well surface using an atomic force microscope

Cited by 73 publications

References 24 publications

Force-distance curves by atomic force microscopy

Force-distance curves by atomic force microscopy

Statistical Analysis of Long- and Short-Range Forces Involved in Bacterial Adhesion to Substratum Surfaces as Measured Using Atomic Force Microscopy

Measuring and visualizing single molecular interactions in biology

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