| Research Title |
Expression and antimicrobial activity of recombinant heteroscorpine-1 from scorpion Heterometrus laoticus toxin |
| Date of Distribution |
14 October 2020 |
| Conference |
| Title of the Conference |
The 4th International Conference on Sustainable Innovation |
| Organiser |
Universitas Muhammadiyah Yogyakarta |
| Conference Place |
Yogyakarta |
| Province/State |
Indonesia |
| Conference Date |
13 October 2020 |
| To |
14 October 2020 |
| Proceeding Paper |
| Volume |
4 |
| Issue |
- |
| Page |
- |
| Editors/edition/publisher |
UMY |
| Abstract |
Scorpion venom is the deadly venom that contains mixture of compound that has been known as a potent source of drug candidate. It have been studied as many objects to explore its pharmacological potential. Heteroscorpine-1 (HS-1), one of the peptide purified from Heterometrus laoticus venom, is one of the scorpion venom components that have an antibacterial activity against Bacillus subtilis, Klebsiella pneumonia, and Pseudomonas aeruginosa. This research, aimed to develop the expression of Heteroscorpine-1 in E. coli system. The genomic sequence of HS-1 was cloned in E. coli DH5α system with pGEM T Easy vector. The cloned gen was ligated to pET32a vector and transformed to E. coli BL21(DE3)pLysS using heat shock method. The positive clone was cultured in LB media with 100 μg/mL Ampicillin. After the OD 600 reached 0.6, the expression was started, induced by Isopropyl β-d-1-thiogalactopyranoside (IPTG). The expressed protein was extracted from the cell and applied to His gravitrap affinity column for protein purification. The fusion protein was identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and liquid chromatography coupled with mass spectrometry (LC-MS/MS). The antimicrobial activity was defined by microdilution method. The recombinant peptide analysis showed that recombinant HS-1 was expressed in the soluble fraction with the band size around 30 kDa, in fusion with thioredoxin tag and histidine tag. The antimicrobial activity test showed that the expressed fusion protein exhibited inhibition. |
| Author |
|
| Peer Review Status |
มีผู้ประเมินอิสระ |
| Level of Conference |
นานาชาติ |
| Type of Proceeding |
Abstract |
| Type of Presentation |
Oral |
| Part of thesis |
true |
| ใช้สำหรับสำเร็จการศึกษา |
ไม่เป็น |
| Presentation awarding |
true |
| Award Title |
Best Presenter |
| Type of award |
รางวัลด้านวิชาการ วิชาชีพ |
| Organiser |
UMY |
| Date of awarding |
14 ตุลาคม 2563 |
| Attach file |
|
| Citation |
0
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Publication
Journal Publication
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