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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...

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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
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Published on: June 23, 2018

Computational methods to predict therapeutic protein aggregation.

Patrick M Buck1, Sandeep Kumar, Xiaoling Wang

  • 1Biotherapeutics Pharmaceutical Research and Development, Pfizer, Inc, St. Louis, MO, USA.

Methods in Molecular Biology (Clifton, N.J.)
|June 28, 2012
PubMed
Summary
This summary is machine-generated.

Computational tools can predict and mitigate protein aggregation, a major challenge for biotherapeutics. Understanding protein aggregation kinetics and stability is key to improving drug product quality and development.

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Area of Science:

  • Biopharmaceutical development
  • Protein aggregation science
  • Computational drug discovery

Background:

  • Protein-based biotherapeutics are vital pharmaceuticals.
  • Physicochemical degradation, especially protein aggregation, impacts drug quality.
  • Predicting and mitigating protein aggregation is critical for biopharmaceutical R&D.

Purpose of the Study:

  • To describe computational tools for understanding and predicting protein aggregation.
  • To categorize these tools into three main classes: unfolding kinetics/thermal stability, colloidal stability, and sequence/structure-based liabilities.
  • To explain the computational methods, their advantages, and limitations.

Main Methods:

  • Review of computational tools for protein aggregation prediction.
  • Classification of tools into three categories based on the aggregation mechanism they address.
  • Detailed explanation of computational methodologies.

Main Results:

  • Identification of computational tools for predicting protein aggregation.
  • Categorization of tools based on their focus: unfolding kinetics, colloidal stability, or sequence/structure liabilities.
  • Discussion of the insights provided by these tools into molecular aggregation events.

Conclusions:

  • Computational tools offer valuable insights into protein aggregation.
  • These tools aid in predicting and potentially mitigating aggregation during biopharmaceutical development.
  • Understanding aggregation mechanisms is crucial for improving drug product quality and formulation.