Enzyme Triggered Gelation of Arginine Containing Ionic-Peptides

We have investigated the possibility of using the protease enzyme thermolysin to catalyse the synthesis and gelation of ionic-complementary peptides from non-gelling peptide precursors. In the described system, thermolysin was added at a fixed concentration (0.3 mg mL−1) to solutions (25 - 100 mg mL−1) of a short tetra-peptide FEFR. Initially, the protease partially hydrolysed the tetrapeptide into di-peptides in all samples. Subsequently, longer peptide sequences were found to form through reverse-hydrolysis and their stability was found to be dependent on their self-assembling properties. The sequences that self-assembled into anti-parallel β-sheet rich fibres became the stable products for the reverse hydrolysis reaction, while the others formed were unstable and disappeared with increasing incubation time. Ultimately, the main product of the system was octa-peptide, which suggests that it represents the thermodynamically favoured product of this dynamic library.