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Recognition Elements PPI Library

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Desirable size of the custom library selection:
  • Mg
  • uMol

ChemDiv’s library of the small molecules affecting protein-protein interactions due to presence of recognition elements contains 23,943 compounds

Protein-protein interactions (PPIs) are crucial for cellular signaling pathways and pivotal processes for disease development such as viral infection, replication, and immune suppression, playing a significant role in the regulation of cellular functions and pathophysiological mechanisms. The exploration of unknown or uncharacterized PPIs within such interaction networks presents an intriguing opportunity for therapeutic intervention and drug discovery. Traditionally, the identification of small molecule modulators for PPIs has been predominantly focused on targets with well-defined structural characteristics. Nevertheless, recent advancements have seen the development of molecular scaffolds designed to mimic the side-chain arrangements of peptide secondary structures, leading to innovative approaches to targeting PPIs.

This innovative toolkit comprises a set of recognition elements, including gamma-turns, beta-turns, and dipeptide mimetics, which are instrumental in replicating the spatial orientation and functionality of peptides. Gamma-turns, involving three amino acid residues, often establish a hydrogen bond between the first and third residues, creating a pseudo-7-membered ring structure that facilitates the reversal of the peptide chain's direction. Similarly, beta-turns, encompassing four residues, can form a hydrogen bond between the first and fourth residues to produce a pseudo-10-membered ring, further contributing to the chain's directional change. To mimic the bioactive conformation of peptides and effectively modulate PPIs, a prevalent strategy involves synthesizing conformationally constrained analogs. These analogs are crafted through backbone-backbone or backbone-side chain cyclization, stabilizing the desired conformation, and enhancing the molecule's ability to modulate complex protein interactions. Such advancements not only broaden the scope of targets amenable to small molecule intervention but also pave the way for discovering novel therapeutics that can modulate intricate biological processes by targeting previously intractable PPIs.

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