Repurpose the antimicrobial peptide Buforin II for plasmid transformation into Escherichia coli
Antimicrobial peptides Buforin II, derived from histone H2A, demonstrates strong cell-penetrating activity without cell lysis and strong affinity for internal cellular nucleic acids, making it a potential candidate for macromolecule delivery into bacteria. Herein, we designed a peptide that is the...
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| Format: | Article |
| Language: | English |
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Can Tho University Publisher
2024-03-01
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| Series: | CTU Journal of Innovation and Sustainable Development |
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| Online Access: | http://web2010.thanhtoan/index.php/ctujs/article/view/659 |
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| _version_ | 1850234967691362304 |
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| author | Thanh Ngoc Nguyen Le Minh Bui |
| author_facet | Thanh Ngoc Nguyen Le Minh Bui |
| author_sort | Thanh Ngoc Nguyen |
| collection | DOAJ |
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Antimicrobial peptides Buforin II, derived from histone H2A, demonstrates strong cell-penetrating activity without cell lysis and strong affinity for internal cellular nucleic acids, making it a potential candidate for macromolecule delivery into bacteria. Herein, we designed a peptide that is the fusion of Buforin II and a polycation tail (KH)6 and assessed its efficiency in delivering plasmid (pGEX-RG-(TAG)5, 7,142 bp) into Escherichia coli OmniMAX. The peptide and plasmid were incubated at 25°C to form the complexes at various peptide concentrations from 5 to 50 µg/mL. After that, the complexes were incubated with the E. coli competent cells at 25°C. In comparison with the transformation efficiency and normalized transformation efficiency of conventional heat-shock method, a 1.28 and 7.83 times higher transformation efficiency, correspondingly, was achieved by using novel peptide-based delivery system at peptide concentration of 5 µg/mL. The cell viability of over 90% was displayed at peptide concentration of 5 µg/mL. This study can lead to the development of a transformation approach under mild conditions and an ideal tool for gene delivery.
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| format | Article |
| id | doaj-art-9adca2bc71f94f34ba3ff39ea40e9d47 |
| institution | OA Journals |
| issn | 2588-1418 2815-6412 |
| language | English |
| publishDate | 2024-03-01 |
| publisher | Can Tho University Publisher |
| record_format | Article |
| series | CTU Journal of Innovation and Sustainable Development |
| spelling | doaj-art-9adca2bc71f94f34ba3ff39ea40e9d472025-08-20T02:02:26ZengCan Tho University PublisherCTU Journal of Innovation and Sustainable Development2588-14182815-64122024-03-01161Repurpose the antimicrobial peptide Buforin II for plasmid transformation into Escherichia coliThanh Ngoc Nguyen0Le Minh Bui1a:1:{s:5:"en_US";s:68:"NTT Hi-Tech Institute, Nguyen Tat Thanh University, Ho Chi Minh City";}NTT Hi-Tech Institute, Nguyen Tat Thanh University, Ho Chi Minh City Antimicrobial peptides Buforin II, derived from histone H2A, demonstrates strong cell-penetrating activity without cell lysis and strong affinity for internal cellular nucleic acids, making it a potential candidate for macromolecule delivery into bacteria. Herein, we designed a peptide that is the fusion of Buforin II and a polycation tail (KH)6 and assessed its efficiency in delivering plasmid (pGEX-RG-(TAG)5, 7,142 bp) into Escherichia coli OmniMAX. The peptide and plasmid were incubated at 25°C to form the complexes at various peptide concentrations from 5 to 50 µg/mL. After that, the complexes were incubated with the E. coli competent cells at 25°C. In comparison with the transformation efficiency and normalized transformation efficiency of conventional heat-shock method, a 1.28 and 7.83 times higher transformation efficiency, correspondingly, was achieved by using novel peptide-based delivery system at peptide concentration of 5 µg/mL. The cell viability of over 90% was displayed at peptide concentration of 5 µg/mL. This study can lead to the development of a transformation approach under mild conditions and an ideal tool for gene delivery. http://web2010.thanhtoan/index.php/ctujs/article/view/659Antimicrobial peptidecell penetrating peptideEscherichia coliplasmidtransformation |
| spellingShingle | Thanh Ngoc Nguyen Le Minh Bui Repurpose the antimicrobial peptide Buforin II for plasmid transformation into Escherichia coli CTU Journal of Innovation and Sustainable Development Antimicrobial peptide cell penetrating peptide Escherichia coli plasmid transformation |
| title | Repurpose the antimicrobial peptide Buforin II for plasmid transformation into Escherichia coli |
| title_full | Repurpose the antimicrobial peptide Buforin II for plasmid transformation into Escherichia coli |
| title_fullStr | Repurpose the antimicrobial peptide Buforin II for plasmid transformation into Escherichia coli |
| title_full_unstemmed | Repurpose the antimicrobial peptide Buforin II for plasmid transformation into Escherichia coli |
| title_short | Repurpose the antimicrobial peptide Buforin II for plasmid transformation into Escherichia coli |
| title_sort | repurpose the antimicrobial peptide buforin ii for plasmid transformation into escherichia coli |
| topic | Antimicrobial peptide cell penetrating peptide Escherichia coli plasmid transformation |
| url | http://web2010.thanhtoan/index.php/ctujs/article/view/659 |
| work_keys_str_mv | AT thanhngocnguyen repurposetheantimicrobialpeptidebuforiniiforplasmidtransformationintoescherichiacoli AT leminhbui repurposetheantimicrobialpeptidebuforiniiforplasmidtransformationintoescherichiacoli |