Enzyme Inhibitory Activities of Marine Sponges Against Cholinesterase and 5α-Reductase
Marine sponges have been the source of various metabolites with potent biological activities. In this study fifteen methanolic extracts of marine sponges, collected off the coast of Tabuhan Island, Banyuwangi, East Java, Indonesia were evaluated in relation to their cholinesterase and 5?-reductase i...
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Malaysian Society of Applied Biology
2019
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id-langga.936212021-10-05T05:13:21Z https://repository.unair.ac.id/93621/ Enzyme Inhibitory Activities of Marine Sponges Against Cholinesterase and 5α-Reductase Suciati, - Karma Rabgay, - Yunda Fachrunniza, - Tongchai Saesong, - Tri Aryono Hadi, - Tutik Sri Wahyuni, - Aty Widyawaruyanti, - Kornkanok Ingkaninan, - R Medicine RS Pharmacy and materia medica Marine sponges have been the source of various metabolites with potent biological activities. In this study fifteen methanolic extracts of marine sponges, collected off the coast of Tabuhan Island, Banyuwangi, East Java, Indonesia were evaluated in relation to their cholinesterase and 5?-reductase inhibitory activities. The results revealed that the extract of Petrosia sp. inhibited the 5?-reductase enzyme at 100 ?g/mL, with 61.21% inhibition, which is slightly lower than the positive control, finasteride, of 76.70%. The results of the cholinesterase inhibitory screening showed that three marine sponges namely, Callyspongia sp., Niphates olemda, and Agelas nakamurai presented notable cholinesterase inhibitory activities. The highest potency was found in A. nakamurai, with an IC50 value of 1.05 ?g/mL. All three samples inhibited both acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE), however, the extract of N. olemda showed a higher inhibition against AChE compared to BuChE. The chemistry of the Callyspongia sp., N. olemda and A. nakamurai were investigated using thin layer chromatography and 1H NMR methods. The results suggested the presence of terpenes and alkaloids in the samples. Further study is needed to determine the metabolite responsible for cholinesterase inhibitory activity. Malaysian Society of Applied Biology 2019-06-30 Article PeerReviewed text en https://repository.unair.ac.id/93621/3/C-13%20Artikel.pdf text en https://repository.unair.ac.id/93621/4/C-13%20Reviewer.pdf text en https://repository.unair.ac.id/93621/2/C-13%20Result.pdf text en https://repository.unair.ac.id/93621/5/C06-ARTIKEL.pdf text en https://repository.unair.ac.id/93621/6/C06-peer%20review.pdf text en https://repository.unair.ac.id/93621/7/C06-similarity.pdf Suciati, - and Karma Rabgay, - and Yunda Fachrunniza, - and Tongchai Saesong, - and Tri Aryono Hadi, - and Tutik Sri Wahyuni, - and Aty Widyawaruyanti, - and Kornkanok Ingkaninan, - (2019) Enzyme Inhibitory Activities of Marine Sponges Against Cholinesterase and 5α-Reductase. Malaysian Applied Biology, 48 (3). pp. 77-83. ISSN 0126-8643 http://www.mabjournal.com/index.php?option=com_content&view=article&id=932&catid=59:current-view&Itemid=56 |
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R Medicine RS Pharmacy and materia medica Suciati, - Karma Rabgay, - Yunda Fachrunniza, - Tongchai Saesong, - Tri Aryono Hadi, - Tutik Sri Wahyuni, - Aty Widyawaruyanti, - Kornkanok Ingkaninan, - Enzyme Inhibitory Activities of Marine Sponges Against Cholinesterase and 5α-Reductase |
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Marine sponges have been the source of various metabolites with potent biological activities. In this study fifteen methanolic extracts of marine sponges, collected off the coast of Tabuhan Island, Banyuwangi, East Java, Indonesia were evaluated in relation to their cholinesterase and 5?-reductase inhibitory activities. The results revealed that the extract of Petrosia sp. inhibited the 5?-reductase enzyme at 100 ?g/mL, with 61.21% inhibition, which is slightly lower than the positive control, finasteride, of 76.70%. The results of the cholinesterase inhibitory screening showed that three marine sponges namely, Callyspongia sp., Niphates olemda, and Agelas nakamurai presented notable cholinesterase inhibitory activities. The highest potency was found in A. nakamurai, with an IC50 value of 1.05 ?g/mL. All three samples inhibited both acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE), however, the extract of N. olemda showed a higher inhibition against AChE compared to BuChE. The chemistry of the Callyspongia sp., N. olemda and A. nakamurai were investigated using thin layer chromatography and 1H NMR methods. The results suggested the presence of terpenes and alkaloids in the samples. Further study is needed to determine the metabolite responsible for cholinesterase inhibitory activity. |
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Article PeerReviewed |
author |
Suciati, - Karma Rabgay, - Yunda Fachrunniza, - Tongchai Saesong, - Tri Aryono Hadi, - Tutik Sri Wahyuni, - Aty Widyawaruyanti, - Kornkanok Ingkaninan, - |
author_facet |
Suciati, - Karma Rabgay, - Yunda Fachrunniza, - Tongchai Saesong, - Tri Aryono Hadi, - Tutik Sri Wahyuni, - Aty Widyawaruyanti, - Kornkanok Ingkaninan, - |
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Suciati, - |
title |
Enzyme Inhibitory Activities of Marine Sponges Against Cholinesterase and 5α-Reductase |
title_short |
Enzyme Inhibitory Activities of Marine Sponges Against Cholinesterase and 5α-Reductase |
title_full |
Enzyme Inhibitory Activities of Marine Sponges Against Cholinesterase and 5α-Reductase |
title_fullStr |
Enzyme Inhibitory Activities of Marine Sponges Against Cholinesterase and 5α-Reductase |
title_full_unstemmed |
Enzyme Inhibitory Activities of Marine Sponges Against Cholinesterase and 5α-Reductase |
title_sort |
enzyme inhibitory activities of marine sponges against cholinesterase and 5α-reductase |
publisher |
Malaysian Society of Applied Biology |
publishDate |
2019 |
url |
https://repository.unair.ac.id/93621/3/C-13%20Artikel.pdf https://repository.unair.ac.id/93621/4/C-13%20Reviewer.pdf https://repository.unair.ac.id/93621/2/C-13%20Result.pdf https://repository.unair.ac.id/93621/5/C06-ARTIKEL.pdf https://repository.unair.ac.id/93621/6/C06-peer%20review.pdf https://repository.unair.ac.id/93621/7/C06-similarity.pdf https://repository.unair.ac.id/93621/ http://www.mabjournal.com/index.php?option=com_content&view=article&id=932&catid=59:current-view&Itemid=56 |
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1713213796184489984 |