Background: Enzymes are proteins that help speed up chemical reactions by creating favourable environment for the conversion of substrates into products. Enzymes are large macromolecules composed of amino acids connected with peptide bonds. Peptides, which are also made up of amino acids, are smaller and easier to synthesize than proteins and can display catalytic properties. Aim: The main purpose of this thesis is to explore the changing of self-assembly and catalytic properties of peptides by introducing amino acid alterations. Methods: Techniques used are solid phase peptide synthesis, liquid chromatography, mass spectrometry, infrared spectroscopy, catalytic kinetic assay and computational molecular dynamics simulation. Results: Two linear and two cyclic peptides were synthesized and characterized. The chromatography data validates the synthesized peptides which proves the possibility of octapeptide on-resin cyclization. Linear peptides formed supramolecular β-sheet-like structures with zinc. Further analysis of the peptides using the catalytic kinetic assay in needed to confirm their catalytic properties. Conclusions: The combination of computational and laboratory techniques is a useful tool in peptide design. Catalytic peptide design is a newly emerging field of study and for this reason, this thesis aims to obtain a better understanding of the matter.