The present study focuses on the initiation phase of protein synthesis and the generation of aptamers as candidates to reduce the physiological function of the isolated N terminal domain (NTD) of initiation factor 3 (IF-3). Through molecular biology techniques, the correct cloning of the gene coding for IF-3 NTD in plasmid pET24a was verified. This plasmid was used to transform the bacterial model organism Escherichia coli BL21 and thus the massive production of the IF-3 NTD was assessed. Using affinity chromatography techniques, the NTD of the IF-3 was isolated, obtaining high purity degrees and production yields. The purified NTD was used to generate aptamers with the SELEX technique (Systematic Evolution of Ligands by Exponential Enrichment). Five molecules with binding potential to the NTD of IF-3 were found. The present investigation provides the bases to study the interaction of the NTD of IF-3 with the aptamers in cell-free system and thus to evaluate their inhibitory potential. It is expected that these molecules behave as potential new drugs, and therefore they might contribute to cope for the need of new antibiotics. / Tesis