Collagen-like polypeptides have attracted significant research attention in recent decades primarily because of potential biological applications, particularly in tissue engineering. The synthesis of novel cyclopolypeptides that would mimic the collagen protein was envisaged. The L-vinylglycine N-carboxyanhydride monomer was synthesised but was found unstable. Later, the project was modified to employ the L-allylglycine N-carboxyanhydride monomer to produce poly(L-allylglycine) with terminal double bonds that were later isomerised into internal alkenes. The isomerised poly(L-allylglycine) was submitted for ring-closing metathesis, utilising a variety of solvent and co-solvent systems with a Grubbs second-generation catalyst, but no reaction occurred. As a result, the approach was further modified to the synthesis of protected dimethoxybenzyl- L-allylglycine N-carboxyanhydride monomer, but the desired polymer could not be synthesised. Finally, to check the feasibility of the RCM step on a small molecule, an L-allylglycine-protected dipeptide was synthesised and isomerised using a Pd catalyst before being subjected to RCM, which was successful in the presence of an excess of Grubbs second-generation catalyst. After deprotection (retaining the Fmoc group) the cyclic dipeptide will be incorporated in a tryptophan zipper to induce a β-turn.