2004
DOI: 10.1016/j.bios.2004.01.012
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Atomic force spectroscopy-based study of antibody pesticide interactions for characterization of immunosensor surface

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Cited by 52 publications
(37 citation statements)
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“…By measuring an in situ membrane protein complex stabilized by the membrane bilayer and by interactions with neighbors, repeated measurements are possible that report functional interactions, with no extraction or unfolding of the cytb 6 f complex. Such stabilizing influences allow measurement of the ;300 pN unbinding forces, which are comparable with those obtained using conventional force spectroscopy for a range of other interactions including 340 to 454 pN for streptavidin-biotin (Lee et al, 1994;Stevens et al, 2002), 507 pN for the hCG-anti-hCG pair (Stevens et al, 2002), 512 pN for the MPAD-anti-MPAD interaction (Kaur et al, 2004), and 420 pN for citrate synthase-GroEL (Vinckier et al, 1998). The forces we measure likely sample the binding interaction prior to electron transfer, given the requirement for both reduced cytb 6 f and oxidized Pc, as well as the similarity of the dwell time (;160 ms at 1.0 kHz force curve repetition rate) of the AFM probe on the membrane surface to the ;70 to 130 ms electron transfer between Pc and cytb 6 f (Haehnel et al, 1980;Delosme, 1991).…”
Section: Affinity-mapping Afm Using Pc-functionalized Afm Probes Allomentioning
confidence: 60%
“…By measuring an in situ membrane protein complex stabilized by the membrane bilayer and by interactions with neighbors, repeated measurements are possible that report functional interactions, with no extraction or unfolding of the cytb 6 f complex. Such stabilizing influences allow measurement of the ;300 pN unbinding forces, which are comparable with those obtained using conventional force spectroscopy for a range of other interactions including 340 to 454 pN for streptavidin-biotin (Lee et al, 1994;Stevens et al, 2002), 507 pN for the hCG-anti-hCG pair (Stevens et al, 2002), 512 pN for the MPAD-anti-MPAD interaction (Kaur et al, 2004), and 420 pN for citrate synthase-GroEL (Vinckier et al, 1998). The forces we measure likely sample the binding interaction prior to electron transfer, given the requirement for both reduced cytb 6 f and oxidized Pc, as well as the similarity of the dwell time (;160 ms at 1.0 kHz force curve repetition rate) of the AFM probe on the membrane surface to the ;70 to 130 ms electron transfer between Pc and cytb 6 f (Haehnel et al, 1980;Delosme, 1991).…”
Section: Affinity-mapping Afm Using Pc-functionalized Afm Probes Allomentioning
confidence: 60%
“…800-1200 pN) (Lee et al, 1994) or immunochemical complex (ca. 60-250 pN) (Kaur et al, 2004), but greater than that required to remove beads bound to the surface by weak, nonspecific interactions (ca. 0.1-10 pN).…”
Section: Resultsmentioning
confidence: 99%
“…Kaur et al (2004) created oriented active immunobiosensor surface by immobilization of antibodies on the gold surface against two herbicide molecules 2,4-dichlorophenoxyacetic acid and atrazine. Analysis of the adhesive forces, between immobilized antibodies and their respective antigens by force spectroscopy using hapten-carrier protein functionalized atomic force microscope (AFM) cantilevers, showed that immobilization had not compromised the reactivity of the surface immobilized antibody molecules for antigen and there was no change in their relative quality with respect to each other.…”
Section: Detection Of Pesticide Residuesmentioning
confidence: 99%