Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Extraction: Partition and Distribution Coefficients01:14

Extraction: Partition and Distribution Coefficients

5.3K
The distribution law or Nernst's distribution law is the law that governs the distribution of a solute between two immiscible solvents. This law, also known as the partition law, states that if a solute is added to the mixture of two immiscible solvents at a constant temperature, the solute is distributed between the two solvents in such a way that the ratio of solute concentrations in the solvents remains constant at equilibrium.
For extracting a solute from an aqueous phase into an...
5.3K
Extraction: Effects of pH00:53

Extraction: Effects of pH

1.5K
Consider a neutral form of an amine, B, with a partition coefficient, K, in a liquid mixture containing organic and aqueous phases. The pH of the aqueous phase affects the charge on acidic and basic solutes, and the charged form is usually more soluble in the aqueous phase. Suppose the conjugate acid form of the amine is soluble only in the aqueous phase while the base form is soluble in both phases. Then the distribution coefficient, D, can be given as the ratio of amine concentration in the...
1.5K
Factors Affecting Dissolution: Drug pKa, Lipophilicity and GI pH01:21

Factors Affecting Dissolution: Drug pKa, Lipophilicity and GI pH

3.9K
Drug absorption within the gastrointestinal (GI) tract is a complex process influenced by several critical factors, including the site pH, the drug's dissociation constant (pKa), and the drug's lipophilicity. The GI tract exhibits a pH gradient, with an acidic environment in the stomach and a more alkaline environment in the small intestine. This pH variation directly affects the ionization state of drugs.
A drug's pKa and the pH of the gastrointestinal (GI) tract play crucial roles...
3.9K
Physiological Pharmacokinetic Models: Assumption with Protein Binding01:13

Physiological Pharmacokinetic Models: Assumption with Protein Binding

326
Physiological models with protein binding in pharmacokinetics offer a sophisticated approach to understanding drug disposition. These models consider drug-protein interactions, enabling them to effectively predict drug concentrations in different organs and tissues. This precision aids in accurate drug dosing, providing a significant advantage over conventional models. A key process within these models is equilibration, which ensures that drug concentrations achieve a steady state within the...
326
Two-Compartment Open Model: Extravascular Administration01:12

Two-Compartment Open Model: Extravascular Administration

783
The two-compartment model for extravascular administration represents a drug's absorption and distribution process. It features a central compartment, where the drug is first absorbed, and a peripheral compartment, which illustrates the drug's distribution throughout the body. The rate of change in drug concentration in the central compartment is calculated by three exponents: absorption, distribution, and elimination.
The absorption exponent (ka) indicates the speed at which the drug...
783
Two-dimensional Gel Electrophoresis01:22

Two-dimensional Gel Electrophoresis

8.0K
Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such...
8.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Osmolyte-Based Formulations for Enhanced Thermal Stability of mRNA Drug Substance: A Systematic Screening and Optimization Study.

Pharmaceutical research·2026
Same author

Quantifying the Acidification-Induced Shift of the Dimerization Equilibrium of PsbS.

The journal of physical chemistry letters·2026
Same author

Development of a 3D Skin Model for Studying Melanoma Progression.

Cells·2026
Same author

Multimodal Chromatography in the Downstream Processing of mAb-Based Products: Mechanisms, Strategies, and Applications.

Biotechnology and bioengineering·2026
Same author

Single-step recovery of mRNA via multimodal chromatography to advance vaccine manufacturing.

Journal of chromatography. A·2025
Same author

Unlocking the potential of extracellular vesicles: one stimulus away from clinical implementation.

Biomaterials science·2025

Related Experiment Video

Updated: Mar 14, 2026

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
11:11

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins

Published on: June 15, 2018

8.8K

Predicting protein partition coefficients in aqueous two phase system.

Dragana P C de Barros1, Sara R R Campos2, Ana M Azevedo3

  • 1iBB-Institute for Bioengineering and Biosciences, Instituto Superior Técnico, University of Lisbon, Av. Rovisco Pais, 1049-001 Lisbon, Portugal; Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.

Journal of Chromatography. A
|October 8, 2016
PubMed
Summary
This summary is machine-generated.

This study explores protein partitioning in aqueous two phase systems (ATPSs) and validates a model predicting protein behavior. The model successfully predicted protein partitioning based on electrostatic and nonpolar interactions.

Keywords:
Aqueous two-phase systemCollander equationPartition coefficient predictionProtein partitioningSemi-empirical model

More Related Videos

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

11.1K
A New Straightforward Method for Lipophilicity logP Measurement using 19F NMR Spectroscopy
09:32

A New Straightforward Method for Lipophilicity logP Measurement using 19F NMR Spectroscopy

Published on: January 30, 2019

15.3K

Related Experiment Videos

Last Updated: Mar 14, 2026

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
11:11

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins

Published on: June 15, 2018

8.8K
Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
09:49

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

11.1K
A New Straightforward Method for Lipophilicity logP Measurement using 19F NMR Spectroscopy
09:32

A New Straightforward Method for Lipophilicity logP Measurement using 19F NMR Spectroscopy

Published on: January 30, 2019

15.3K

Area of Science:

  • Biochemistry
  • Chemical Engineering
  • Separation Science

Background:

  • Aqueous two phase systems (ATPSs) are utilized for protein separation.
  • Predicting protein partitioning behavior in ATPSs is crucial for process optimization.
  • Existing models may not fully capture the complex interactions governing protein partitioning.

Purpose of the Study:

  • To gain further insight into protein partitioning behavior within ATPSs.
  • To evaluate the effectiveness of a semi-empirical model for predicting protein partition coefficients.
  • To investigate the influence of protein properties and ATPS characteristics on partitioning.

Main Methods:

  • Partitioning of 14 globular proteins was studied in three polymer/polymer ATPSs.
  • A semi-empirical model based on continuum electrostatics was employed for prediction.
  • The Collander equation was used to analyze correlations in partitioning coefficients.

Main Results:

  • A linear correlation was observed between protein partitioning coefficients across different ATPSs.
  • The semi-empirical model demonstrated the ability to predict protein partitioning behavior.
  • Electrostatic energy correlated with protein size and ATPS properties, while nonpolar energy correlated with solvent accessible surface area.
  • Polymer structure and concentration significantly impacted model performance.

Conclusions:

  • The semi-empirical model provides a valuable tool for predicting protein partitioning in ATPSs.
  • Protein partitioning is influenced by electrostatic and nonpolar interactions, as well as system parameters.
  • The study offers a good qualitative prediction of protein phase preference in ATPSs.