In resent years peptides have been shown to be more important that what it was previously believed in both plant and animal growth and development. This as well as the pharmaceutical and industrial applications of peptides have led to improved large scale production and purification of these compounds. Generally production of peptides intended for in vitro research, regulation of cell physiology and therapeutic applications, follows one of two main methods: chemical synthesis or hetrologous expression. Yet expression of very short polypeptide chains can sometimes be problematic in microbial systems, including in bacterial cells such as Escherichia coli . In these cases the use of tandem repeat of peptide units or insertion of fusion partners may increase expression efficiency. In the present study MBP8298, a 17-amino acid peptide, was selected as a model peptide for a study of heterologous expression in E. coli . Nucleotide coding sequence of MBP8298 was designed and synthesized based on the bacterial codon usage, mRNA secondary structure, as well as the required nucleotide restriction sites and polypeptide cleavage points. A nucleotide sequence encoding a fusion partner (based on the sequence by Paulus et al , 2004 and hence named Paulus Sequence) was also constructed the same gene synthesis technology. The fusion partner was subsequently attached upstream of two concatemers of MBP8298 coding sequence that in turn had a downstream 6His tag coding sequence. This construct, dubbed PM 2 H (comprising Paulus + 2 MBP8298 + 6His) was then cloned into a pET-21c(+) expression vector. The Paulus Sequence encodes an AU-rich sequence just after the start codon, followed by a stem-loop in the mRNA structure and is reported to increase expression of downstream polypeptides probably because of enhanced translation initiation. For comparison purposes two other constructs were also prepared. First, one named M 2 H, that had a similar structure to PM 2 H but lacked the Paulus Sequence and second, another one named UM 2 H that contained ubiquitin ORF (Isolated from Medicago truncatula ) in place of the Paulus Sequence. Once sequencing of the constructs were confirmed, they were transformed into the expression hosts BL21(DE3) and subsequently induced with IPTG to produce the recombinant proteins. Analysis of expressed proteins, by SDS-PAGE, indicated that UM 2 H and PM 2 H were present as soluble and inclusion body respectively. No expression of M 2 H was detected. Expressed fusion proteins were purified by Ni affinity batch chromatography (which in turn verified the expected presence of C-terminal His tags). In summary it was shown that both fusion partners (Paulus Sequence and ubiqutin) markedly increase the MBP8298 expression level that was otherwise non detectable