Finding new small molecules able to disrupt protein-protein interactions is challenging. Starting from natural ligands is a good solution if the problem of their instability in biological media is controlled. Several strategies were used to design these libraries of peptidomimetic compounds.

Unnatural amino acids can be synthesized using the Petasis reaction, a multiple component reaction involving an amine, an acid and a boronic acid. Starting from secondary amines and glyoxylic acid, original diakylaminoamides can be efficiently obtained. These small acids can fool the proteases recognition sites to stabilize the molecule in vivo. Related active compounds can be found in enzyme inhibitors, ion channels regulators, GPCR antagonists and some antibacterials.

Our selection of peptidomimetics was based on scaffolds that mimic beta-turns: spiropyrrolidinones, tetrahydrocarbolines, hexahydro-pyrazinopyrimidinediones, hexahydro-thiazolopyridinones, original benzodiazepines, spirohydantoines and spirothiazolidines. Original dihydrooxadiazolines were added since this heterocycle is a good isostere of a peptide linking. A selection of focused fragments and of molecules containing at least two peptidic bounds was also selected to optimize the diversity of the library.
   
Details and scientific references can be found in the dialkylaminoamide library brochure and in the peptidomimetic selection brochure.

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