Survey of the year 2006 commercial optical biosensor literature

Rich, Rebecca L.; Myszka, David G.

doi:10.1002/jmr.862

Cited by 108 publications

(77 citation statements)

References 1,198 publications

(220 reference statements)

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“…Moreover, for binding to occur according to this mechanism, GPIbα surface density should not be less than required to maintain a distance between two molecules compatible with the concurrent binding of one FIIa molecule. Based on crystal structure dimensions and predicted 1 pg∕mm 2 bound protein per RU measured in SPR, such critical density may be as high as 4 • 10 9 GPIbα-N molecules∕mm 2 ; however, functionally efficient clustering appears to occur even at 1∕4th such density, likely explained by the known fluidity and mobility of the dextran surface of SPR chips to which molecules are anchored (38).…”

Section: Discussionmentioning

confidence: 99%

Binding of α-thrombin to surface-anchored platelet glycoprotein Ibα sulfotyrosines through a two-site mechanism involving exosite I

Zarpellon

Celikel

Roberts

et al. 2011

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

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The involvement of exosite I in α-thrombin (FIIa) binding to platelet glycoprotein Ibα (GPIbα), which could influence interactions with other substrates, remains undefined. To address the problem, we generated the GPIbα amino terminal domain (GPIbα-N) fully sulfated on three tyrosine residues and solved the structure of its complex with FIIa. We found that sulfotyrosine (Tys) 278 enhances the interaction mainly by establishing contacts with exosite I. We then evaluated how substituting tyrosine with phenylalanine, which cannot be sulfated, affects FIIa binding to soluble or surface-immobilized GPIbα-N. Mutating Tyr 276 , which mostly contacts exosite II residues, markedly reduced FIIa interaction with both soluble and immobilized GPIbα-N; mutating Tyr 278 or Tyr 279 , which mostly contact exosite I residues, reduced FIIa complexing in solution by 0-20% but affinity for immobilized GPIbα-N 2 to 6-fold, respectively. Moreover, three exosite I ligands-aptamer HD1, hirugen, and lepirudin-did not interfere with soluble FIIa complexing to GPIbα-N, excluding that their binding caused allosteric effects influencing the interaction; nonetheless, all impaired FIIa binding to immobilized GPIbα-N and platelet GPIb nearly as much as aptamer HD22 and heparin, both exosite II ligands. Bound HD1 and hirugen alter Trp 148 orientation in a loop near exosite I preventing contacts with the sulfate oxygen atoms of Tys 279 . These results support a mechanism in which binding occurs when the two exosites of one FIIa molecule independently interact with two immobilized GPIbα molecules. Through exosite engagement, GPIbα may influence FIIa-dependent processes relevant to hemostasis and thrombosis.tyrosine sulfation | tyrosylprotein sulfotransferase-2 | protease-activated receptor | platelet activation | platelet aggregation

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Section: Discussionmentioning

confidence: 99%

Binding of α-thrombin to surface-anchored platelet glycoprotein Ibα sulfotyrosines through a two-site mechanism involving exosite I

Zarpellon

Celikel

Roberts

et al. 2011

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

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“…5 presents a summary of all 25 SPR experiments corresponding to all possible combinations studied, including homotypic interactions. It is important to note that SPR is not the technique of choice to study homodimerization events (31), and the corresponding sensorgrams are presented here for sake of completeness only. The phenomenon of homodimerization was dealt with above when describing the SV-AUC and CD data.…”

Section: Surface Plasmon Resonancementioning

confidence: 99%

Heterotypic Coiled-Coil Formation is Essential for the Correct Assembly of the Septin Heterofilament

Sala

Valadares

Macêdo

et al. 2016

Biophysical Journal

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Protein-protein interactions play a critical role in promoting the stability of protein quaternary structure and in the assembly of large macromolecular complexes. What drives the stabilization of such assemblies is a central question in biology. A limiting factor in fully understanding such systems is the transient nature of many complexes, making structural studies difficult. Septins comprise a conserved family of guanine nucleotide binding proteins that polymerize in the form of heterofilaments. In structural terms, they have a common organization: a central GTPase domain, an N-terminal domain, and a C-terminal domain; the latter is predicted to form a coiled coil. Currently, even for the best characterized human septin heterocomplex (SEPT2/SEPT6/SEPT7), the role of C-terminal domain is not fully established, and this is partly due to the absence of electron density for the C-terminal domains in the x-ray structure. Here we present results on the homo/heterotypical affinity for the C-terminal domains of human septins belonging to the SEPT6 and SEPT7 groups (SEPT6C/8C/10C/11C and SEPT7C, respectively) and provide clear evidence that this domain determines the preference for heterotypic interactions at one specific interface during the assembly of the heterofilament. This observation has wider implications where macromolecular assemblies are defined by coiled-coil protein interactions.

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“…The hydrogel requires only very small amount of protein for immobilization due to the electrostatic attraction between the protein molecules and dextran. Moreover, it suspends the ligand in the solution Rich and Myszka, 2007). Yet, the use of hydrogel also comes with the limitation of handling more complex crude substances due to non specific adsorption (Shankaran and Miura, 2007) and also due to increase in non specific adsorption with respect to time of usage (Masson et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

“…In some cases, non specific adsorption can be reduced by adding CM dextran sodium salt in the samples (Karlsson et al, 1993;Yang et al, 2005). To date, BIAcore and CM5 chip are most widely used equipment and sensor chip (Rich and Myszka, 2005;Rich and Myszka, 2007).…”

Section: Introductionmentioning

confidence: 99%

A simple method for quantification of interferon-2b through surface plasmon resonance technique

Ramanan¹,

Ling²,

Tey³

et al. 2010

Afr. J. Biotechnol.

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A rapid and efficient immunoassay method for quantification of interferon-α2b using surface plasmon resonance was developed with BIAcore 3000 as a sensor. Two different levels of anti-interferon monoclonal antibody were immobilized onto a CM5 chip using an amine coupling method. Similar binding ratio was observed for both the ligand densities. There was no steric hindrance and loss of antibody activity even at higher ligand density (> 22,000 RU). The sensitivity of the assay was increased up to 45% with the increment in ligand density from 15,400 to 22,360 RU. The binding between interferon-α2b and anti-interferon monoclonal antibody was predominantly controlled by mass transfer rate and the relationship was found linear, ranged from 5 to 400 ng/mL. Total cycle time per analysis was less than 8 min and required only 5 µL of sample injection.

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Survey of the year 2006 commercial optical biosensor literature

Cited by 108 publications

References 1,198 publications

Binding of α-thrombin to surface-anchored platelet glycoprotein Ibα sulfotyrosines through a two-site mechanism involving exosite I

Binding of α-thrombin to surface-anchored platelet glycoprotein Ibα sulfotyrosines through a two-site mechanism involving exosite I

Heterotypic Coiled-Coil Formation is Essential for the Correct Assembly of the Septin Heterofilament

A simple method for quantification of interferon-2b through surface plasmon resonance technique

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