Novel Therapeutic Property of Recombinant Human GAPDH Peptide

The development of new antimicrobial agents from natural resources by genetic engineering methods has become a trend in biotech research today. There are enormous numbers of peptide and proteins present in plants, animals, and microbial system that has the specific ability in inducing innate immunity as well as controlling the growth of infectious agents. In the present study the partial Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) gene of size 584 bp (94-677) from the full coding region of human system was amplified, cloned and sequenced. The sequence analysis of the gene exhibits the psuedogene nature with five stop codons at positions 328, 331, 502, 553, 557. Based on the cutting site of the restriction enzyme HindIII exclusively at 198 position a fragment of 104 bp (94-198) was selected and expressed in prokaryotic system. The recombinant GAPDH peptide was purified. The bactericidal property of the recombinant GAPDH peptide alone and its synergistic effect with the antibiotic ampicillin were confirmed by the Antibacterial sensitivity test (AST). The presence of positive charged aminoacids lysine and the hydrophobic aminoacids isoleucine, valine and tyrosine in the recombinant GAPDH peptide strongly supports the mode of action of the peptide in suppressing the bacterial growth.