Peptides have the capability to adopt several positions in the binding sites. This flexibility is a real advantage for first intention screenings when few information about the active site is available. But due to their poor metabolic stability, peptides have to be modified to become interesting leads.

In a strategy related to the design of our dialkylaminoamide library, we focused this library around alkylonitrile and aminoamides compounds. Several examples of alkylonitrile compounds were described as cathepsin and dipeptidyl peptidase inhibitors. The main challenge of those series is to achieve selectivity by finely tuning the substituants close to the nitrile. We designed eight original scaffolds to address this problem.

The ethylenediamine linker is often used to design pro-drugs. Numerous bio-active compounds contain this linkage, including some antihistaminics. Our objective was to introduce a substitution on the link to improve its stability towards proteases.

Details and scientific references can be found in the peptide surrogate library brochure.

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