Binding Kinetics and Footprinting ofTaqI Endonuclease:  Effects of Metal Cofactors on Sequence-Specific Interactions†

Biochemistry ◽  
1999 ◽  
Vol 38 (25) ◽  
pp. 8080-8087 ◽  
Author(s):  
Weiguo Cao
Keyword(s):  
Binding Kinetics ◽  
Specific Interactions ◽  
Metal Cofactors

scholarly journals Antibody-Hapten Recognition at the Surface of Functionalized Liposomes Studied by SPR: Steric Hindrance of Pegylated Phospholipids in Stealth Liposomes Prepared for Targeted Radionuclide Delivery

2011 ◽  
Vol 2011 ◽  
pp. 1-9 ◽  
Author(s):  
Eliot. P. Botosoa ◽  
Mike Maillasson ◽  
Marie Mougin-Degraef ◽  
Patricia Remaud-Le Saëc ◽  
Jean-François Gestin ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Steric Hindrance ◽  
Lipid Fraction ◽  
Binding Kinetics ◽  
Specific Interactions ◽  
Pegylated Liposomes ◽  
Stealth Liposomes ◽  
Indium Complex ◽  
Pegylated Lipids ◽  
Pegylated Phospholipids

Targeted PEGylated liposomes could increase the amount of drugs or radionuclides delivered to tumor cells. They show favorable stability and pharmacokinetics, but steric hindrance of the PEG chains can block the binding of the targeting moiety. Here, specific interactions between an antihapten antibody (clone 734, specific for the DTPA-indium complex) and DTPA-indium-tagged liposomes were characterized by surface plasmon resonance (SPR). Non-PEGylated liposomes fused on CM5 chips whereas PEGylated liposomes did not. By contrast, both PEGylated and non-PEGylated liposomes attached to L1 chips without fusion. SPR binding kinetics showed that, in the absence of PEG, the antibody binds the hapten at the surface of lipid bilayers with the affinity of the soluble hapten. The incorporation of PEGylated lipids hinders antibody binding to extents depending on PEGylated lipid fraction and PEG molecular weight. SPR on immobilized liposomes thus appears as a useful technique to optimize formulations of liposomes for targeted therapy.

Binding kinetics of fluorescent bisphosphonates as a tool for monitoring bone dynamics in vivo

2013 ◽  
Author(s):  
Robert Tower ◽  
Graeme Campbell ◽  
Marc Muller ◽  
Olga Will ◽  
Frederieka Grundmann ◽  
...  
Keyword(s):  
Binding Kinetics ◽  
Kinetics Of ◽  
Bone Dynamics

Influence of Brain Gangliosides on the Formation and Properties of Supported Lipid Bilayers for Binding Kinetics Studies

2018 ◽  
Author(s):  
Luke Jordan ◽  
Nathan Wittenberg
Keyword(s):  
Lipid Bilayers ◽  
Binding Kinetics ◽  
Supported Lipid Bilayers ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Supported Lipid Bilayer ◽  
Head Groups ◽  
Lipid Diffusion ◽  
Kinetics Of ◽  
Brain Gangliosides

This is a comprehensive study of the effects of the four major brain gangliosides (GM1, GD1b, GD1a, and GT1b) on the adsorption and rupture of phospholipid vesicles on SiO2 surfaces for the formation of supported lipid bilayer (SLB) membranes. Using quartz crystal microbalance with dissipation monitoring (QCM-D) we show that gangliosides GD1a and GT1b significantly slow the SLB formation process, whereas GM1 and GD1b have smaller effects. This is likely due to the net ganglioside charge as well as the positions of acidic sugar groups on ganglioside glycan head groups. Data is included that shows calcium can accelerate the formation of ganglioside-rich SLBs. Using fluorescence recovery after photobleaching (FRAP) we also show that the presence of gangliosides significantly reduces lipid diffusion coefficients in SLBs in a concentration-dependent manner. Finally, using QCM-D and GD1a-rich SLB membranes we measure the binding kinetics of an anti-GD1a antibody that has similarities to a monoclonal antibody that is a hallmark of a variant of Guillain-Barre syndrome.

Fragment MO Calculations on Specific Interactions between AhR and TCDD for Beluga and Tern

2009 ◽  
Vol 10 ◽  
pp. 63-75
Author(s):  
Satoshi Miyagi ◽  
Eri Yoshikawa ◽  
Kenichi Dedachi ◽  
Satoshi Itoh ◽  
Mitsuko Ishihara-Sugano ◽  
...  
Keyword(s):  
Specific Interactions ◽  
Mo Calculations
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