Two synthetic genes that code for artificial proteins have been constructed that were modeled on the most regularly repeated hydrophobic domain of human tropoelastin. We compare the physicochemical properties of the recombinant products that differ in their primary structure; the alanine/lysine-rich cross-linking domains, which are highly conserved in mammalian tropoelastin, were either present or absent in the recombinant products. Both biopolymers showed thermoresponsive properties, and variations were observed that were dependent on solution conditions. Cell compatibility was assayed using the biopolymers as coating agents in culture experiments with a neuroblastoma cell line; cell adhesion and proliferation effects were evaluated. The cells were found to retain their neural differentiation potential. The data presented in our work support the usefulness of these versatile biopolymers for a variety of applications related to biotechnology and biomedicine.