Identification of an inter-cysteine loop potentially involved in the activity of Opisthorchis viverrini-granulin-1
Aim: Identification of small bioactive regions in proteins and peptides can be useful information in drug design studies. The current study has shown that an inter-cysteine loop of the N-terminal domain of Opisthorchis viverrini granulin-1 (Ov-GRN-1), a granulin protein from the flatworm liver fluke...
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| Format: | Article |
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Open Exploration
2023-06-01
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| Series: | Exploration of Drug Science |
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| Online Access: | https://www.explorationpub.com/uploads/Article/A100812/100812.pdf |
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| author | Rozita Takjoo David T. Wilson Paramjit S. Bansal Alex Loukas Michael J. Smout Norelle L. Daly |
| author_facet | Rozita Takjoo David T. Wilson Paramjit S. Bansal Alex Loukas Michael J. Smout Norelle L. Daly |
| author_sort | Rozita Takjoo |
| collection | DOAJ |
| description | Aim: Identification of small bioactive regions in proteins and peptides can be useful information in drug design studies. The current study has shown that an inter-cysteine loop of the N-terminal domain of Opisthorchis viverrini granulin-1 (Ov-GRN-1), a granulin protein from the flatworm liver fluke Opisthorchis viverrini which has potent wound healing properties, maintains the bioactivity of the full-length protein. Methods: Peptides corresponding to the three inter-cysteine loops of the N-terminal domain were produced using synthetic chemistry, and their structures and bioactivities were analyzed using nuclear magnetic resonance (NMR) spectroscopy and cell proliferation assays, respectively. Results: As expected for such small peptides, NMR analysis indicated that the peptides were poorly structured in solution. However, a seven-residue peptide corresponding to loop 2 (GRN-L2) promoted cell proliferation, in contrast to the other fragments. Conclusions: The results from the current study suggest that GRN-L2 might be responsible, in part, for the bioactivity of Ov-GRN-1, and might be a useful lead molecule for subsequent wound healing studies. |
| format | Article |
| id | doaj-art-85aae21b318147cd8bb3c4f050e961b0 |
| institution | Kabale University |
| issn | 2836-7677 |
| language | English |
| publishDate | 2023-06-01 |
| publisher | Open Exploration |
| record_format | Article |
| series | Exploration of Drug Science |
| spelling | doaj-art-85aae21b318147cd8bb3c4f050e961b02025-02-08T05:16:47ZengOpen ExplorationExploration of Drug Science2836-76772023-06-011317217910.37349/eds.2023.00012Identification of an inter-cysteine loop potentially involved in the activity of Opisthorchis viverrini-granulin-1Rozita Takjoo0https://orcid.org/0000-0002-1527-4026David T. Wilson1https://orcid.org/0000-0001-5047-0711Paramjit S. Bansal2Alex Loukas3https://orcid.org/0000-0002-0896-8441Michael J. Smout4https://orcid.org/0000-0001-6937-0112Norelle L. Daly5https://orcid.org/0000-0002-4697-6602Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaAustralian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaAustralian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaAustralian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaAustralian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaAustralian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaAim: Identification of small bioactive regions in proteins and peptides can be useful information in drug design studies. The current study has shown that an inter-cysteine loop of the N-terminal domain of Opisthorchis viverrini granulin-1 (Ov-GRN-1), a granulin protein from the flatworm liver fluke Opisthorchis viverrini which has potent wound healing properties, maintains the bioactivity of the full-length protein. Methods: Peptides corresponding to the three inter-cysteine loops of the N-terminal domain were produced using synthetic chemistry, and their structures and bioactivities were analyzed using nuclear magnetic resonance (NMR) spectroscopy and cell proliferation assays, respectively. Results: As expected for such small peptides, NMR analysis indicated that the peptides were poorly structured in solution. However, a seven-residue peptide corresponding to loop 2 (GRN-L2) promoted cell proliferation, in contrast to the other fragments. Conclusions: The results from the current study suggest that GRN-L2 might be responsible, in part, for the bioactivity of Ov-GRN-1, and might be a useful lead molecule for subsequent wound healing studies.https://www.explorationpub.com/uploads/Article/A100812/100812.pdfgranulinpeptideoxidative foldingnuclear magnetic resonance spectroscopycell proliferation |
| spellingShingle | Rozita Takjoo David T. Wilson Paramjit S. Bansal Alex Loukas Michael J. Smout Norelle L. Daly Identification of an inter-cysteine loop potentially involved in the activity of Opisthorchis viverrini-granulin-1 Exploration of Drug Science granulin peptide oxidative folding nuclear magnetic resonance spectroscopy cell proliferation |
| title | Identification of an inter-cysteine loop potentially involved in the activity of Opisthorchis viverrini-granulin-1 |
| title_full | Identification of an inter-cysteine loop potentially involved in the activity of Opisthorchis viverrini-granulin-1 |
| title_fullStr | Identification of an inter-cysteine loop potentially involved in the activity of Opisthorchis viverrini-granulin-1 |
| title_full_unstemmed | Identification of an inter-cysteine loop potentially involved in the activity of Opisthorchis viverrini-granulin-1 |
| title_short | Identification of an inter-cysteine loop potentially involved in the activity of Opisthorchis viverrini-granulin-1 |
| title_sort | identification of an inter cysteine loop potentially involved in the activity of opisthorchis viverrini granulin 1 |
| topic | granulin peptide oxidative folding nuclear magnetic resonance spectroscopy cell proliferation |
| url | https://www.explorationpub.com/uploads/Article/A100812/100812.pdf |
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