Synthesis of N-linked glycopeptides on solid support and their evaluation as protease substrates.

A range of glycopeptides containing protease cleavage sites were synthesized on solid support using Fmoc-based solid phase glycopeptide synthesis. The immobilized peptides were studied as substrates for the proteases chymotrypsin and thermolysin. For chymotrypsin, N-glycosylation of an Asn residue at the P(2) site appears to reduce hydrolysis whereas glycosylation of the P(1) site does not appear to affect peptide hydrolysis by thermolysin.