Trypsin (EC 3.4.21.4), an endopeptidase and natural protease found in the digestive system, cleaves peptide chains and proteins predominantly at the carboxyl side of the amino acids Lys and Arg (except when followed by Pro). Peptides and proteins are gaining importance as modern biopharmaceuticals, due to their high specifity and efficacy. One drawback, however, is their low stability and resulting unfavourable pharmacokinetics. Proteases such as trypsin, in fact, degrade peptides and proteins rather rapidly decreasing in this way their bioavailability. It has, however, been demonstrated that shorter homologues of arginine built into model peptides will increase their stability accordingly. Similar effects have been observed whenever the guanidine side chain has been modified.

With our proprietary arginine platform we can design arginine derivatives bearing substitutions on the guanidine nitrogen from any commercially available amine. A process is available to provide Fmoc and Pbf protected derivatives, which can instantly be used in any Fmoc/tBu solid phase peptide synthesis protocol.