What are the applications of Protein- protein interaction with respect of bioinformatics, drug designing, inhibitor screening and cancer studying
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Answer:
Protein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that occur in a cell or in a living organism in a specific biomolecular context.[1]
The horseshoe shaped ribonuclease inhibitor (shown as wireframe) forms a protein–protein interaction with the ribonuclease protein. The contacts between the two proteins are shown as coloured patches.
Proteins rarely act alone as their functions tend to be regulated. Many molecular processes within a cell are carried out by molecular machines that are built from numerous protein components organized by their PPIs. These interactions make up the so-called interactomics of the organism, while aberrant PPIs are the basis of multiple aggregation-related diseases, such as Creutzfeldt–Jakob, Alzheimer's diseases.
PPIs have been studied with many methods and from different perspectives: biochemistry, quantum chemistry, molecular dynamics, signal transduction, among others.[2][3] All this information enables the creation of large protein interaction networks[4] – similar to metabolic or genetic/epigenetic networks – that empower the current knowledge on biochemical cascades and molecular etiology of disease, as well as the discovery of putative protein targets of therapeutic interest.
Answer:
Protein–protein interactions (PPIs) act as regulatory nodes in many cell-signaling networks linked to the “hallmarks of cancer.” A number of PPIs strongly linked to cell signaling and cell survival have been identified and validated as therapeutic targets for cancer, and have become the focus of academic and industry drug discovery programs. Small-molecule PPI inhibitors have been discovered via high-throughput screening, rational design, virtual screening, or fragment screens. Small-molecule inhibitors of Bcl-2 family PPIs, the MDM2–p53 PPI, and Smac-IAP family PPIs have been developed and have commenced clinical trials. The structural diversity of inhibitors of other PPI cancer targets is illustrated.
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