Characterization of the Properties of Cocaine in Blood: Blood Clearance, Blood to Plasma Ratio, and Plasma Protein Binding

1996 ◽  
Vol 85 (6) ◽  
pp. 567-571 ◽  
Author(s):  
Juthamas Sukbuntherng ◽  
Debra K. Martin ◽  
Yvonne Pak ◽  
Michael Mayersohn
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Blood Clearance ◽  
Plasma Ratio

scholarly journals Ultrafiltration Method for Plasma Protein Binding Studies and Its Limitations

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 382
Author(s):  
Camelia-Maria Toma ◽  
Silvia Imre ◽  
Camil-Eugen Vari ◽  
Daniela-Lucia Muntean ◽  
Amelia Tero-Vescan
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Specific Binding ◽  
Critical Role ◽  
Volume Ratio ◽  
Binding Studies ◽  
Experimental Conditions ◽  
Key Aspects

Plasma protein binding plays a critical role in drug therapy, being a key part in the characterization of any compound. Among other methods, this process is largely studied by ultrafiltration based on its advantages. However, the method also has some limitations that could negatively influence the experimental results. The aim of this study was to underline key aspects regarding the limitations of the ultrafiltration method, and the potential ways to overcome them. The main limitations are given by the non-specific binding of the substances, the effect of the volume ratio obtained, and the need of a rigorous control of the experimental conditions, especially pH and temperature. This review presents a variety of methods that can hypothetically reduce the limitations, and concludes that ultrafiltration remains a reliable method for the study of protein binding. However, the methodology of the study should be carefully chosen.

scholarly journals Plasma protein binding in uremia: Extraction and characterization of an inhibitor

1980 ◽  
Vol 18 (1) ◽  
pp. 86-94 ◽  
Author(s):  
Thomas A. Depner ◽  
Paul F. Gulyassy ◽  
Linda A. Stanfel ◽  
Elizabeth A. Jarrard
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein

Evaluation of electrophoretic mobility shift assay as a method to determine plasma protein binding of siRNA

Bioanalysis ◽  
2019 ◽  
Vol 11 (21) ◽  
pp. 1927-1939 ◽  
Author(s):  
Carrie Rocca ◽  
Sean Dennin ◽  
Yongli Gu ◽  
Joohwan Kim ◽  
Samantha Chigas ◽  
...  
Keyword(s):  
Protein Binding ◽  
Electrophoretic Mobility Shift Assay ◽  
Electrophoretic Mobility ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Small Interfering Rnas ◽  
Mobility Shift ◽  
Mobility Shift Assay

Aim: The electrophoretic mobility shift assay (EMSA) was evaluated as an alternative to ultrafiltration (UF) to assess plasma protein binding (PPB) of small interfering RNAs (siRNA) and antisense oligonucleotides (ASO). Results & methodology: EMSA analysis showed that PPB depended on siRNA and plasma concentration. Conversely, when analyzed by ultrafiltration, siRNA bound the filtration device nonspecifically and PPB remained >98% across physiologically relevant siRNA concentrations. Using EMSA, siRNA exhibited charge-based interactions with plasma proteins, while ASO remained highly bound to plasma proteins or albumin in the presence of 500 mM salt. Conclusion: PPB characteristics of siRNA and ASO can be distinguished using EMSA. Characterization of siRNA PPB by EMSA enhances our knowledge of siRNA absorption, distribution, metabolism and excretion and advanced development of RNA interference therapeutics.

Synthesis, Radiolabeling, and Characterization of Plasma Protein-Binding Ligands: Potential Tools for Modulation of the Pharmacokinetic Properties of (Radio)Pharmaceuticals

2017 ◽  
Vol 28 (9) ◽  
pp. 2372-2383 ◽  
Author(s):  
Cristina Müller ◽  
Renáta Farkas ◽  
Francesca Borgna ◽  
Raffaella M. Schmid ◽  
Martina Benešová ◽  
...  
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Pharmacokinetic Properties

scholarly journals Characterization of Binding of Raltegravir to Plasma Proteins

2013 ◽  
Vol 57 (10) ◽  
pp. 5147-5150 ◽  
Author(s):  
Caroline Barau ◽  
Valérie Furlan ◽  
Yazdan Yazdanpanah ◽  
Catherine Fagard ◽  
Jean-Michel Molina ◽  
...  
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Association Constant ◽  
Graphical Method ◽  
Acid Glycoprotein ◽  
Ph Increase

ABSTRACTThe objective of this study was to characterize raltegravir (RAL) binding to albumin and alpha-1-acid glycoprotein (AAG). Unbound and bound RAL were separated by ultrafiltration. The association constant (Ka) was estimated by a graphical method. In HIV-infected patients, the average plasma protein binding is 76%. RAL did not bind to AAG but bound to nonsaturable, low-affinity albumin sites with ann(number of sites) ·Kaproduct of 9.8 × 102liters/mol. A pH increase of 0.2 U led to a 2% increase in the bound fraction.

scholarly journals Characterization of plasma protein binding dissociation with online SPE-HPLC

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Ping Li ◽  
Yiran Fan ◽  
Yunlong Wang ◽  
Yaxin Lu ◽  
Zheng Yin
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Online Spe

scholarly journals Characterization of chloroquine plasma protein binding in man.

1983 ◽  
Vol 15 (3) ◽  
pp. 375-377 ◽  
Author(s):  
O Walker ◽  
DJ Birkett ◽  
G Alvan ◽  
LL Gustafsson ◽  
F Sjoqvist
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein

Characterization of plasma protein binding in two mouse models of humanized liver, PXB mouse and humanized TK-NOG mouse

Xenobiotica ◽  
2020 ◽  
Vol 51 (1) ◽  
pp. 51-60
Author(s):  
Maki Miyamoto ◽  
Yohei Kosugi ◽  
Shinji Iwasaki ◽  
Ikumi Chisaki ◽  
Sayaka Nakagawa ◽  
...  
Keyword(s):  
Protein Binding ◽  
Mouse Models ◽  
Plasma Protein Binding ◽  
Plasma Protein

scholarly journals Blood to Plasma Ratio, Short-Term Stability and Plasma Protein Binding of Casiopeína IIgly, a Copper (II) Based Compound with Antineoplastic Activity

2017 ◽  
Vol 57 (3) ◽  
Author(s):  
Roberto Carlos Cañas-Alonso ◽  
Inés Fuentes-Noriega ◽  
Lena Ruiz-Azuara
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Whole Blood ◽  
High Plasma ◽  
Antineoplastic Activity ◽  
Preclinical Studies ◽  
Short Term ◽  
Plasma Ratio ◽  
Term Stability

Casiopeína IIgly is a mixed chelate coordination compound with copper (II) core that has shown important antineoplastic activity, even in some resistant cellular lines to Cisplatin. In this work, preclinical studies as blood to plasma ratio, plasma protein binding, short-term stability in blood and pharmacokinetics of this coordination complex are reported. The results indicate that Casiopeína IIgly is stable in blood at least for 6 hours at 37 °C. Also, this compound exhibits an important accumulation in whole blood rather than plasma fluid, a high plasma protein binding (>90%) as well as short half-life (47 min).

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