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Related Concept Videos

Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

Factors Affecting Protein-Drug Binding: Protein-Related Factors

Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be bound by...
Factors Affecting Protein-Drug Binding: Drug-Related Factors01:18

Factors Affecting Protein-Drug Binding: Drug-Related Factors

Drug binding to proteins is a complex phenomenon influenced by various drug-related factors, each playing a significant role in the interaction between drugs and proteins within the body.
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In contrast,...
Factors Affecting Protein-Drug Binding: Patient-Related Factors01:29

Factors Affecting Protein-Drug Binding: Patient-Related Factors

Protein-drug binding, a pivotal aspect of pharmacokinetics, is subject to considerable variability influenced by an array of patient-related factors. The intricate interplay of age, individual differences, and pathological conditions significantly impact the binding dynamics and subsequent pharmacological effects.
Age stands as a key determinant in protein-drug binding. Neonates, characterized by low albumin content, experience heightened concentrations of unbound drugs such as phenytoin and...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...

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Related Experiment Video

Updated: Jul 3, 2026

Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor
07:59

Extraction and Visualization of Protein Aggregates after Treatment of Escherichia coli with a Proteotoxic Stressor

Published on: June 29, 2021

Some factors determining protein aggregation during ultrafiltration.

K J Kim1, V Chen, A G Fane

  • 1Centre for Membrane Science and Technology, School of Chemical Engineering and Industrial Chemistry, University of New South Wales, Kensington, NSW 2033, Australia.

Biotechnology and Bioengineering
|June 20, 1993
PubMed
Summary
This summary is machine-generated.

Protein aggregation during albumin ultrafiltration is caused by rapid supersaturation and high shear near the membrane. Shear forces likely unfold proteins, promoting particle collisions and flocculation, impacting filtration efficiency.

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Area of Science:

  • Biochemistry
  • Chemical Engineering
  • Materials Science

Background:

  • Protein aggregation is a critical issue in ultrafiltration processes, affecting efficiency and product purity.
  • Albumin ultrafiltration is widely used in biopharmaceutical manufacturing and medical applications.

Purpose of the Study:

  • To investigate the factors influencing protein aggregation during albumin ultrafiltration.
  • To understand the role of operational conditions on protein deposit formation.

Main Methods:

  • Studied protein aggregation under varying operational conditions.
  • Utilized electron microscopy to characterize the nature of protein deposits.

Main Results:

  • Protein aggregation is linked to rapid protein supersaturation near the membrane surface.
  • High solvent velocity (shear) in the concentrated layer exacerbates aggregation.
  • Shear forces appear to unfold protein molecules, promoting particle flocculation.

Conclusions:

  • Rapid supersaturation and high shear are key drivers of protein aggregation in albumin ultrafiltration.
  • Membrane surface shear plays a significant role in protein unfolding and subsequent aggregation.
  • Understanding these factors is crucial for optimizing ultrafiltration processes and preventing fouling.