scholarly journals Rapid Equilibrium Dialysis (RED): an In-vitro High-Throughput Screening Technique for Plasma Protein Binding using Human and Rat Plasma

2012 ◽  
Vol s14 ◽  
Author(s):  
Jitendra Kumar Singh ◽  
Anant Solanki
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
High Throughput ◽  
Plasma Protein ◽  
High Throughput Screening ◽  
Equilibrium Dialysis ◽  
Rat Plasma ◽  
Screening Technique ◽  
Rapid Equilibrium

Validation of a Rapid Equilibrium Dialysis Approach for the Measurement of Plasma Protein Binding

2008 ◽  
Vol 97 (10) ◽  
pp. 4586-4595 ◽  
Author(s):  
Nigel J. Waters ◽  
Rachel Jones ◽  
Gareth Williams ◽  
Bindi Sohal
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Equilibrium Dialysis ◽  
Rapid Equilibrium

scholarly journals Evaluation of the Pharmacokinetics of the Pancreastatin Inhibitor PSTi8 Peptide in Rats: Integration of In Vitro and In Vivo Findings

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 339
Author(s):  
Guru R. Valicherla ◽  
Roshan A. Katekar ◽  
Shailesh Dadge ◽  
Mohammed Riyazuddin ◽  
Anees A. Syed ◽  
...  
Keyword(s):  
Gender Difference ◽  
Protein Binding ◽  
Blood Plasma ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Liver Microsomes ◽  
Rat Plasma ◽  
Dose Proportionality

PSTi8 is a pancreastatin inhibitory peptide that is effective in the treatment of diabetic models. This study investigates the pharmacokinetic (PK) properties of PSTi8 in Sprague Dawley rats, for the first time. In vitro and in vivo PK studies were performed to evaluate the solubility, stability in plasma and liver microsomes, plasma protein binding, blood–plasma partitioning, bioavailability, dose proportionality, and gender difference in PK. Samples were analyzed using the validated LC-MS/MS method. The solubility of PSTi8 was found to be 9.30 and 25.75 mg/mL in simulated gastric and intestinal fluids, respectively. The protein binding of PSTi8 was estimated as >69% in rat plasma. PSTi8 showed high stability in rat plasma and liver microsomes and the blood–plasma partitioning was >2. The bioavailability of PSTi8 after intraperitoneal and subcutaneous administration was found to be 95.00 ± 12.15 and 78.47 ± 17.72%, respectively, in rats. PSTi8 showed non-linear PK in dose proportionality studies, and has no gender difference in the PK behavior in rats. The high bioavailability of PSTi8 can be due to high water solubility and plasma protein binding, low clearance and volume of distribution. Our in vitro and in vivo findings support the development of PSTi8 as an antidiabetic agent.

Solid-phase microextraction for assessment of plasma protein binding, a complement to rapid equilibrium dialysis

Bioanalysis ◽  
2021 ◽  
Author(s):  
Sheelan Ahmad ◽  
Daniel Baker ◽  
Darragh Murnane ◽  
Neil Spooner ◽  
Ute Gerhard
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Solid Phase Microextraction ◽  
Solid Phase ◽  
Equilibrium Dialysis ◽  
Free Concentration ◽  
Rapid Equilibrium

Aim: Determination of plasma protein binding ( PPB) is considered vital for better understanding of pharmacokinetic and pharmacodynamic activities of drugs due to the role of free concentration in pharmacological response. Methodology & results: Solid-phase microextraction (SPME) was investigated for measurement of PPB from biological matrices and compared with a gold standard approach (rapid equilibrium dialysis [RED]). Discussion & conclusion: SPME-derived values of PPB correlated well with literature values, and those determined by RED. Respectively, average protein binding across three concentrations by RED and SPME was 33.1 and 31.7% for metoprolol, 89.0 and 86.6% for propranolol and 99.2 and 99.0% for diclofenac. This study generates some evidence for SPME as an alternative platform for the determination of PPB.

scholarly journals Prediction of drug-drug plasma protein binding interactions of resveratrol in combination with celecoxib and leflunomide by molecular docking combined with an ultrafiltration technique

2020 ◽  
Vol 70 (1) ◽  
pp. 111-119 ◽  
Author(s):  
Peng Zhou ◽  
Fang Hua
Keyword(s):  
Hydrogen Bond ◽  
Molecular Docking ◽  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Molecular Interactions ◽  
Computational Prediction ◽  
Rat Plasma ◽  
Drug Plasma

AbstractThe present study is aimed at computational prediction of the molecular interactions between resveratrol, celecoxib, leflunomide and human serum albumin (HSA) and then investigates the plasma protein binding of resveratrol combined with celecoxib or leflunomide by an ultrafiltration technique. Molecular operating environment (MOE, 2008.10) software package was used to explore molecular interactions between the drugs and HSA. Molecular docking was adopted to predict the interactions between resveratrol and other drugs and then the ultrafiltration technique was used to verify the docking results. In in vitro experiments, a mixture of resveratrol and celecoxib or leflunomide was added to rat plasma for determination of the plasma protein binding rate. Molecular docking results have shown that resveratrol interacts with HSA mainly through hydrogen bond and π-π stacking, while celecoxib and leflunomide bind only with the hydrogen bond. Celecoxib or leflunomide, even at high tested doses, did not affect the plasma protein binding of resveratrol, thus suggesting pharmacological suitability of the investigated combinations.

scholarly journals Metabolism and plasma protein binding of 16 straight- and branched-chain parabens in in vitro liver and skin models

2020 ◽  
pp. 105051
Author(s):  
Cathy Lester ◽  
Nicola J. Hewitt ◽  
Ursula Müller-Vieira ◽  
Manuela Mayer ◽  
Corie Ellison ◽  
...  
Keyword(s):  
Protein Binding ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Branched Chain
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