On the Calculation of the Concentration Dependence of Drug Binding to Plasma Proteins with Multiple Binding Sites of Different Affinities: Determination of the Possible Variation of the Unbound Drug Fraction and Calculation of the Number of Binding Sites of the Protein

2007 ◽  
Vol 96 (2) ◽  
pp. 249-257 ◽  
Author(s):  
Leonid M. Berezhkovskiy
Keyword(s):  
Concentration Dependence ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Drug Binding ◽  
Multiple Binding Sites ◽  
Multiple Binding ◽  
Number Of Binding Sites

Equilibrium dialysis, ultrafiltration, and ultracentrifugation compared for determining the plasma-protein-binding characteristics of valproic acid.

1985 ◽  
Vol 31 (1) ◽  
pp. 60-64 ◽  
Author(s):  
J Barré ◽  
J M Chamouard ◽  
G Houin ◽  
J P Tillement
Keyword(s):  
Valproic Acid ◽  
Human Serum Albumin ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Equilibrium Dialysis ◽  
Anticonvulsant Drug ◽  
Drug Binding ◽  
Binding Characteristics ◽  
Affinity Constants ◽  
Number Of Binding Sites

Abstract Equilibrium dialysis, ultrafiltration, and ultracentrifugation were compared to determine their reliability and applicability in the study of binding of an anticonvulsant drug, valproic acid, by plasma proteins. We studied drug binding with pooled serum and with solutions of human serum albumin at physiological concentrations. We compared binding characteristics such as number of binding sites, affinity constants, and percent of binding as measured by each method in the therapeutic range for valproic acid. Results by ultracentrifugation differed from those by equilibrium dialysis and ultrafiltration, which agreed reasonably well with each other.

NMDAR PAMs: Multiple Chemotypes for Multiple Binding Sites

2019 ◽  
Vol 19 (24) ◽  
pp. 2239-2253 ◽  
Author(s):  
Paul J. Goldsmith
Keyword(s):  
Binding Sites ◽  
Receptor Activation ◽  
Research Area ◽  
Allosteric Modulators ◽  
Nonselective Cation Channels ◽  
Multiple Binding Sites ◽  
Multiple Binding ◽  
Excitatory Neurotransmission ◽  
Psychiatric Conditions ◽  
High Level

The N-methyl-D-aspartate receptor (NMDAR) is a member of the ionotropic glutamate receptor (iGluR) family that plays a crucial role in brain signalling and development. NMDARs are nonselective cation channels that are involved with the propagation of excitatory neurotransmission signals with important effects on synaptic plasticity. NMDARs are functionally and structurally complex receptors, they exist as a family of subtypes each with its own unique pharmacological properties. Their implication in a variety of neurological and psychiatric conditions means they have been a focus of research for many decades. Disruption of NMDAR-related signalling is known to adversely affect higherorder cognitive functions (e.g. learning and memory) and the search for molecules that can recover (or even enhance) receptor output is a current strategy for CNS drug discovery. A number of positive allosteric modulators (PAMs) that specifically attempt to overcome NMDAR hypofunction have been discovered. They include various chemotypes that have been found to bind to several different binding sites within the receptor. The heterogeneity of chemotype, binding site and NMDAR subtype provide a broad landscape of ongoing opportunities to uncover new features of NMDAR pharmacology. Research on NMDARs continues to provide novel mechanistic insights into receptor activation and this review will provide a high-level overview of the research area and discuss the various chemical classes of PAMs discovered so far.

Effects of Multiple Binding Sites on Studies of Hydrogen Bonding between Nitroxide Radicals and Solvent Molecules

1993 ◽  
Vol 58 (1) ◽  
pp. 47-52 ◽  
Author(s):  
Imad Al-Bala'a ◽  
Richard D. Bates
Keyword(s):  
Hydrogen Bonding ◽  
Magnetic Resonance ◽  
Binding Site ◽  
Binding Sites ◽  
Hyperfine Coupling Constant ◽  
Hydrogen Donor ◽  
Complex Formation Constants ◽  
Multiple Binding Sites ◽  
Multiple Binding ◽  
Solvent Molecules

The role of more than one binding site on a nitroxide free radical in magnetic resonance determinations of the properties of the complex formed with a hydrogen donor is examined. The expression that relates observed hyperfine couplings in EPR spectra to complex formation constants and concentrations of each species in solution becomes much more complex when multiple binding sites are present, but reduces to a simpler form when binding at the two sites occurs independently and the binding at the non-nitroxide site does not produce significant differences in the hyperfine coupling constant in the complexed radical. Effects on studies of hydrogen bonding between multiple binding site nitroxides and hydrogen donor solvent molecules by other magnetic resonance methods are potentially more extreme.

Creating BHb-imprinted magnetic nanoparticles with multiple binding sites

The Analyst ◽  
2017 ◽  
Vol 142 (2) ◽  
pp. 302-309 ◽  
Author(s):  
Yanxia Li ◽  
Yiting Chen ◽  
Lu Huang ◽  
BenYong Lou ◽  
Guonan Chen
Keyword(s):  
Magnetic Nanoparticles ◽  
Binding Sites ◽  
Multifunctional Nanoparticles ◽  
Multiple Binding Sites ◽  
Multiple Binding

A kind of protein imprinted over magnetic Fe3O4@Au multifunctional nanoparticles (NPs) with multiple binding sites was synthesized and investigated.

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