| dc.description.abstract | Antimicrobial peptides (AMPs) are small, cationic peptides that have gained
attention as a potential alternative to antibiotics due to their broad-spectrum activity
against bacteria, fungi, and viruses. Porcine PG-1 is an AMP that has shown promise
as a therapeutic agent. However, recombiant production if this AMP is challenging
due to its inherit toxicity to the host cells. In this study, we aimed to enhance the sta bility and prevent the toxicity of PG-1 by fusing it with a carrier protein. Specifically,
to clone porcine antimicrobial peptide PG-1 into the unstructured regions of a carrier
protein. Through a screening process, a suitable insertion site within TOI29 DNA Poly merase was identified, replacing the unstructured region of Terminal protein region 2
(TPR2). This fusion protein complex has the potential to improve the solubility and
stability of PG1 as well as reducing its’ inherent toxicity towards microbial host cells.
The gene encoding the carrier protein was inserted into the expression vector prior to
the insertion of PG-1 using recombinant DNA technology. Experimental procedures
involved the finding of insertion site on carrier protein embedded in expression vec tors, obtain purified Polymerase Chain Reaction (PCR) product of insert and vector,
cloning of PG-1 into the carrier protein, checking the expression of the fusion protein
in host cells via ligation products. This recombinant fusion protein was expressed in E.
coli, and its expression was evaluated using growth inhibition assays of Kanamycin on
DH5α Escherichia Coli (E.coli) strain. Unfortunately, the study ended with variations
in the final step when the final results do not align. However, these achievement shows
promising application of utilizing fusion protein approach in recombinant technology
to produce AMP with low cost and high efficiency. | en_US |
