The recombinant expression and antimicrobial activity determination of Cecropin-like part of Heteroscorpine-1 from Heterometrus laoticus

Abstract. Erviana R, Saengkun Y, Rungsa P, Jangpromma N, Mustofa, Daduang S. 2022. The recombinant expression and antimicrobial activity determination of Cecropin-like part Heteroscorpine-1 from Heterometrus laoticus. Biodiversitas 23: 5646-5653. Antimicrobial peptides are promising novel antibiotics that hold great potential in combating bacteria, fungi, viruses, parasites. Recent interest has increased their as new pharmacological agents. Large quantities required order to fulfill the demand for scientific research clinical trials. Gene systems have been developed, which may be utilized efficiently various peptide-related studies applications. However, many developed require steps impact cost. This study established fast easy system (CeHS-1) determined activity. gene was chemically synthesized, ligated vector pET32a, transformed Escherichia coli BL21 (DE3) pLysS competent cell, induced by 0.2 mM isopropyl ?-D-1-thiogalactopyranoside. induction time optimization 3 hrs resulted highest yield. prolonged would decrease yield due toxicity toward host cells. peptide purification facilitated His tag sequence through purifying affinity chromatographic column Ni-NTA. able express expected soluble fraction. assay showed could inhibit growth bacterial strains. lower compared synthetic peptides. finding demonstrated this might facilitate feasible CeHS-1. Additionally, revealed expressed preserved.