Force Spectroscopy and Dynamics of the BiotinAvidin Bond Studied by Scanning Force Microscopy

París, Roberto; Strunz, Torsten; Oroszlan, Krisztina; Güntherodt, H.‐J.; Hegner, Martin

doi:10.1002/1438-5171(200012)1:4<285::aid-simo285>3.3.co;2-v

Cited by 18 publications

(36 citation statements)

References 9 publications

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“…6(a,b)]. Although last ruptures are thought to correspond to individual unbinding events, 24 as far as fibrinogen adsorption is concerned it is likely that we are not measuring the unbinding from the surface of a single amino acid but rather the rupture of a group of amino acids.…”

Section: Discussionmentioning

confidence: 99%

AFM force spectroscopy of the fibrinogen adsorption process onto dental implants

Boukari¹,

Francius

Hemmerlé

2006

J Biomedical Materials Res

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Protein binding to implants is governed by the physicochemical properties of the biomaterial surface. The adhesion of a protein onto a solid surface is nonspecific. The aim of this study was to assess the adsorption process of fibrinogen at two different dental implants. The first biomaterial has a sand-blasted titanium surface, whereas the second one is covered by a calcium phosphate coating. After scanning electron microscopy and atomic force microscopy characterization of the implant surfaces, force spectroscopy has been used to determine the unbinding force of fibrinogen adsorbed at the two different substrates. Force-measurement findings indicate that the detachment force of fibrinogen adsorbed onto both surfaces varies as a function of the interaction time. The mean strength of the unbinding forces increases with the interaction time (100 and 1,000 ms, respectively). However, experimental data suggest that fibrinogen fixes to the two studied biomaterials by different mechanisms. Moreover, it appears that, after an interaction time of 1,000 ms, the detachment force of the adsorbed protein is quite larger for the titanium surface than for the calcium phosphate coating.

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Section: Discussionmentioning

confidence: 99%

AFM force spectroscopy of the fibrinogen adsorption process onto dental implants

Boukari¹,

Francius

Hemmerlé

2006

J Biomedical Materials Res

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“…A logarithmic dependence of the forces on the loading rate was found in systems close to thermodynamical equilibrium, where a single energy barrier governs the separation process (Carrion-Vasquez et al, 1999;Fritz et al, 1998;Rief et al, 1997;Schwesinger et al, 2000). In contrast, force spectroscopy on biotin/ avidin and biotin/streptavidin complexes revealed the influence of multiple energy barriers on the unbinding mechanism of these systems (De Paris et al, 2000;Merkel et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Specific binding of the regulatory protein ExpG to promoter regions of the galactoglucan biosynthesis gene cluster of Sinorhizobium meliloti - a combined molecular biology and force spectroscopy investigation

Bartels

Baumgarth

Anselmetti

et al. 2003

Journal of Structural Biology

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Specific protein-DNA interaction is fundamental for all aspects of gene transcription. We focus on a regulatory DNA-binding protein in the Gram-negative soil bacterium Sinorhizobium meliloti 2011, which is capable of fixing molecular nitrogen in a symbiotic interaction with alfalfa plants. The ExpG protein plays a central role in regulation of the biosynthesis of the exopolysaccharide galactoglucan, which promotes the establishment of symbiosis. ExpG is a transcriptional activator of exp gene expression. We investigated the molecular mechanism of binding of ExpG to three associated target sequences in the exp gene cluster with standard biochemical methods and single molecule force spectroscopy based on the atomic force microscope (AFM). Binding of ExpG to expA1, expG-expD1, and expE1 promoter fragments in a sequence specific manner was demonstrated, and a 28 bp conserved region was found. AFM force spectroscopy experiments confirmed the specific binding of ExpG to the promoter regions, with unbinding forces ranging from 50 to 165 pN in a logarithmic dependence from the loading rates of 70-79 000 pN/s. Two different regimes of loading rate-dependent behaviour were identified. Thermal off-rates in the range of k off ¼ ð1:2 AE 1:0Þ Â 10 À3 s À1 were derived from the lower loading rate regime for all promoter regions. In the upper loading rate regime, however, these fragments exhibited distinct differences which are attributed to the molecular binding mechanism.

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“…The k syst values were obtained from the slope of each retraction curve immediately prior to the unbinding event. [29][30][31] All blocking experiments were conducted at the nominal loading rate of 7 nN/s.…”

mentioning

confidence: 99%

Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy

Bizzarri

Santini

Coppari

et al. 2011

IJN

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p28 is a 28-amino acid peptide fragment of the cupredoxin azurin derived from Pseudomonas aeruginosa that preferentially penetrates cancerous cells and arrests their proliferation in vitro and in vivo. Its antitumor activity reportedly arises from post-translational stabilization of the tumor suppressor p53 normally downregulated by the binding of several ubiquitin ligases. This would require p28 to specifically bind to p53 to inhibit specific ligases from initiating proteosome-mediated degradation. In this study, atomic force spectroscopy, a nanotechnological approach, was used to investigate the interaction of p28 with full-length p53 and its isolated domains at the single molecule level. Analysis of the unbinding forces and the dissociation rate constant suggest that p28 forms a stable complex with the DNA-binding domain of p53, inhibiting the binding of ubiquitin ligases other than Mdm2 to reduce proteasomal degradation of p53.

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Force Spectroscopy and Dynamics of the BiotinAvidin Bond Studied by Scanning Force Microscopy

Cited by 18 publications

References 9 publications

AFM force spectroscopy of the fibrinogen adsorption process onto dental implants

AFM force spectroscopy of the fibrinogen adsorption process onto dental implants

Specific binding of the regulatory protein ExpG to promoter regions of the galactoglucan biosynthesis gene cluster of Sinorhizobium meliloti - a combined molecular biology and force spectroscopy investigation

Interaction of an anticancer peptide fragment of azurin with p53 and its isolated domains studied by atomic force spectroscopy

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