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Updated: May 21, 2026
08:38
Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
Published on: March 3, 2015
Protein-protein interactions: network analysis and applications in drug discovery
Jennyfer Bultinck1, Sam Lievens, Jan Tavernier
1Department of Medical Protein Research, VIB, Ghent, Belgium.
Current Pharmaceutical Design
|June 2, 2012
Summary
Mapping protein-protein interactions (PPIs) is crucial for discovering new therapeutic targets. Combining experimental and computational methods enhances biological network resolution for identifying disease-related proteins and PPIs.
Area of Science:
- Biochemistry
- Molecular Biology
- Systems Biology
Background:
- Protein-protein interactions (PPIs) are fundamental to cellular processes.
- Targeting PPIs presents therapeutic opportunities but faces challenges, especially with small molecules.
- Accurate protein interaction networks are essential for drug discovery and therapeutic target identification.
Purpose of the Study:
- To highlight the importance of comprehensive human and pathogen protein interaction maps.
- To discuss current methodologies for mapping protein-protein interactions.
- To emphasize the need for improved coverage and resolution in protein networks.
Main Methods:
- Literature curation and computational approaches for network generation.
- Experimental methods, notably yeast two-hybrid (Y2H) technology, for mapping PPIs.
- Integration of diverse genetic and biochemical techniques to enhance network data.
Main Results:
- Yeast two-hybrid (Y2H) technology has demonstrated reliability in producing protein networks.
- A combination of methods is being employed to generate biological networks.
- Ongoing efforts aim to increase the coverage and resolution of protein interaction maps.
Conclusions:
- Detailed protein interaction maps are vital starting points for PPI inhibitor screening and design.
- Advancements in mapping PPIs will facilitate the identification of novel disease-related proteins.
- Enhanced protein networks hold significant potential for developing new therapeutic strategies targeting PPIs.
Related Concept Videos
02:04Protein-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...
02:04Protein-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...
02:26Protein 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.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
02:26Protein 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.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
01:22Protein-Drug Binding: Determination Methods
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...
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...
01:16Protein-Drug Binding: Mechanism and Kinetics
Protein-drug binding refers to the interaction between drugs and proteins within the body. This binding process can occur intracellularly, involving drug interactions with enzymes or receptors within cells, or extracellularly, involving plasma proteins in the blood.
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...