We proposed a novel synthetic method for artificial extracellular matrices using a synthesis of repetitive DNA library. The overlap elongation PCR was used to synthesize repetitive DNA library from short nucleotide duplex as a starting duplex. Using this new method, we created repetitive DNA libraries encoding elastin-derived structural motif (VPGVG) and collagen like sequence containing Arg-Gly-Asp (RGD) cell adhesive motif (GERGDRGDP), isolated repetitive DNA coded 16-times VPGVG (Ela-16) and 5-times GERGDRGDP (Col-5) and overexpressed these repetitive sequences as fusion proteins with thioredoxin. These artificial recombinant proteins were well produced by Eschelicia coli expression system. A cell adhesion test using mouse fibroblast NIH/3T3 cells revealed that Col-5 protein having multi RGD motifs fulfilled function of a cell adhesive reagent. The structural features of these proteins were analyzed by scanning electron microscopy (SEM). SEM observation revealed that Ela-16 precipitant was fibrous, and oppositely Col-5 precipitant had network granular feature. These differences of structural features could be brought from the insertion of repetitive amino acid sequences created by overlap elongation PCR. Thus, using this new method we can easily acquire various functional and structural proteins containing repetitive amino acid sequences.