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Protein-Protein Interaction Library

Designed for discovery of novel PPI inhibitors

59 370 compounds

Having a pivotal role in multiple cellular processes, protein-protein interactions (PPIs) are responsible for the effects linked to the blockage of the substrate binding site. There are numerous examples of drug candidates that were withdrawn from clinical trials due to the unexpected effects of direct antagonists. This fact outlines the importance of developing new potent protein-protein interactions inhibitors.

We have carefully selected 59 370 diverse compounds specifically targeting PPIs. All compounds are stored as dry materials and they can be acquired in diverse custom formats. Using our PPI Library for hit discovery you receive multiple benefits allowing you to save on time and costs in lead generation:

  • Dry stock of over 2.6M compounds for hit resupply and hit expansion.
  • Low-cost synthesis of analogues within only 3 weeks through our REAL Database technology
  • Medicinal chemistry support enhanced with on-site broad ADME/T panel

You have also an option to screen the Library directly at Enamine. In this case, we will be happy to offer discount on library cost depending on the collaboration scope.

Most popular library formats

Item
Catalog No.
Compounds
Plates
Amount
Format

Item

1

Catalog No.

PPI-52-Y-0

Compounds

52 160

Plates

163

Amount

Any suitable for 1 assay

Format

384-well microplates, 320 cpds per plate,
first two and last two columns empty

Item

2

Catalog No.

PPI-52-Z-10

Compounds

52 160

Plates

41

Amount

10 µL of 10 mM
DMSO stock solutions

Format

1536-well microplates, Echo Qualified,
1280 cmpds per plate, first four and last four columns empty

Item

3

Catalog No.

PPI-52-Y-50

Compounds

52 160

Plates

163

Amount

50 µL of 10 mM
DMSO solutions

Format

384-well microplates, 320 cpds per plate,
first two and last two columns empty

Library Design

Systemic analysis of published data on thermodynamic, structural and pharmacological aspects of numerous PPIs on both pro- and eukaryotic proteomes, as well as viral PPIs allowed us to develop a dedicated approach to the PPI library design. We have analyzed more than 20 protein-protein complexes to define specific features of the most potent inhibitors in this area. Several specific recognition patterns that were highlighted are α-helix, β-sheet (Ab), PDZ-, Armadillo/HEAT - (β-catenin), Polo-box - domains -mediated PPIs.

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