We demonstrate that protease can be used to trigger the synthesis of ionic complementary peptides and above a critical peptide concentration this results in a sol-gel transition. Upon addition of the protease the tetra peptide FEFK partially hydrolyses to FE and FK and this subsequently encourages the synthesis of hexa, octa and decapeptide through reverse hydrolysis. The octapeptide is the most favored product probably due to its high self-assembling ability as once formed they self-assemble and become trapped into β-sheet rich nanofibers that subsequently entangle to form a self-supporting, elastic hydrogel. This novel method opens up the possibility of synthesizing a diverse library of ionic peptides that undergo a sol-gel transition with no harsh chemicals and water being the only by-product.
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