Tropoelastin is the dominant monomer that assembles to form elastin, which confers elasticity to vertebrate elastic tissues including skin, arteries and lungs. This thesis explores regions in tropoelastin that are involved in cell binding. Cell interactions with tropoelastin were probed by utilising a total of 15 recombinant tropoelastin constructs, which contain different domains of tropoelastin. Through sequential analyses of these constructs’ ability to interact with cells, multiple regions of cell interaction were identified. One of these cell interactive sequences in tropoelastin was mapped to domain 17 and the first 6 amino acids (aa) of domain 18. A peptide made to this region promoted cell attachment and spreading independently. Inhibition studies involving heparan sulfate, EDTA and anti-integrin antibodies revealed a possible two-step mechanism by which cell interactions occur at this region: initially, cell adhesion is mediated by glycosaminoglycans (GAGs), which contact the lysine residues within the target sequence, and subsequently facilitate cell spreading modulated by integrins, specifically αvβ3 and αvβ5. Further studies confirmed integrin-mediated binding site/s in domains 12-16, independent from domains 17-18. Domain 12-16 was found to interact through both the integrin αv family and integrin α5β1, whereas integrin α5β1 only inhibited in combination with integrin αv. On this basis a model was developed where the αv integrins initially engage with tropoelastin, which then allows for integrin α5β1 engagement, further strengthening the tropoelastin-cell interaction. This work identifies for the first time multiple sites in tropoelastin in the central region of tropoelastin. Discovering novel cell adhesion sequences and understanding the mechanisms involved in the interaction would substantially contribute to the next generation of biomaterials and provide a platform for future studies to understand biochemical pathways in the matrix biology field.