Technical data on the inhibition properties of some medicinal plant extracts towards caseinolytic protease proteolytic subunit of Plasmodium knowlesi
Proteolytic subunit of the caseinolytic protease system of Plasmodium knowlesi (Pk-ClpP; EC 3.4.21.92) is considered a viable target for antimalarial drug development to eradicate P. knowlesi malaria infection in Malaysia and Southeast Asian region. Inhibition of this system leads to a disruption in...
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| Format: | Article |
| Language: | English |
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Elsevier
2021-12-01
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| Series: | Data in Brief |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340921008635 |
| _version_ | 1818873892893097984 |
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| author | Raimalynah Abd Razak Meiny Suzery Rafida Razali Zarina Amin Ruzaidi Azli Mohd Mokhtar Ping Chin Lee Cahyo Budiman |
| author_facet | Raimalynah Abd Razak Meiny Suzery Rafida Razali Zarina Amin Ruzaidi Azli Mohd Mokhtar Ping Chin Lee Cahyo Budiman |
| author_sort | Raimalynah Abd Razak |
| collection | DOAJ |
| description | Proteolytic subunit of the caseinolytic protease system of Plasmodium knowlesi (Pk-ClpP; EC 3.4.21.92) is considered a viable target for antimalarial drug development to eradicate P. knowlesi malaria infection in Malaysia and Southeast Asian region. Inhibition of this system leads to a disruption in the protein homeostasis molecular machinery and therefore be lethal for the parasite. While plants are considered excellent sources of bioactive compounds exhibiting inhibition activity towards Pk-ClpP, many local medicinal plants remain unexplored. This article expands the data collected from the inhibition properties of the methanolic extract of Asystasia gangetica (Chinese Violet), Alstonia scholaris (Pulai Tree), Piper retrofractum (Javanese Long Pepper) and Smallanthus sonchifolius (Yacon) towards Pk-ClpP. These plants are widely found in Malaysia and Indonesia and have been traditionally used in various medical treatments. The present dataset showed that the extracts contained phenolic and flavonoid compounds in various concentrations, whereby S. sonchifolius was found to have the lowest content of phenolic and flavonoid contents, while A. gangetica and A. scholaris were statistically comparable, yet higher than P. retrofactum and S. sonchifolus. Further inhibition data assay towards Pk-ClpP revealed that A. gangetica, A. scholaris and P. retrofactum demonstrated remarkable inhibition activity with IC50 values of 39.06 ± 1.98, 48.92 ± 1.52, and 87.63 ± 3.55, respectively. However, the inhibition activity of these extracts was significantly lower than a serine protease inhibitor of phenylmethylsulfonyl fluoridenone (PMSF). Meanwhile, S. sonchifolus did not exhibit significant inhibition activity towards Pk-ClpP. In addition, Pk-ClpP was not inhibited by a cysteine protease inhibitor of E64. |
| first_indexed | 2024-12-19T13:01:56Z |
| format | Article |
| id | doaj.art-a0e2b997ddd3433abc5b6b23f2aa7a81 |
| institution | Directory Open Access Journal |
| issn | 2352-3409 |
| language | English |
| last_indexed | 2024-12-19T13:01:56Z |
| publishDate | 2021-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Data in Brief |
| spelling | doaj.art-a0e2b997ddd3433abc5b6b23f2aa7a812022-12-21T20:20:14ZengElsevierData in Brief2352-34092021-12-0139107588Technical data on the inhibition properties of some medicinal plant extracts towards caseinolytic protease proteolytic subunit of Plasmodium knowlesiRaimalynah Abd Razak0Meiny Suzery1Rafida Razali2Zarina Amin3Ruzaidi Azli Mohd Mokhtar4Ping Chin Lee5Cahyo Budiman6Biotechnology Research Institute, University Malaysia Sabah, Jalan UMS, Kota Kinabalu, Sabah 88400, MalaysiaDepartment of Chemistry, Faculty of Sciences and Mathematics, Diponegoro University, Jl. Prof. Soedarto, SH, Tembalang, Semarang 50275, IndonesiaBiotechnology Research Institute, University Malaysia Sabah, Jalan UMS, Kota Kinabalu, Sabah 88400, MalaysiaBiotechnology Research Institute, University Malaysia Sabah, Jalan UMS, Kota Kinabalu, Sabah 88400, MalaysiaBiotechnology Research Institute, University Malaysia Sabah, Jalan UMS, Kota Kinabalu, Sabah 88400, MalaysiaBiotechnology Research Institute, University Malaysia Sabah, Jalan UMS, Kota Kinabalu, Sabah 88400, MalaysiaBiotechnology Research Institute, University Malaysia Sabah, Jalan UMS, Kota Kinabalu, Sabah 88400, Malaysia; Corresponding author.Proteolytic subunit of the caseinolytic protease system of Plasmodium knowlesi (Pk-ClpP; EC 3.4.21.92) is considered a viable target for antimalarial drug development to eradicate P. knowlesi malaria infection in Malaysia and Southeast Asian region. Inhibition of this system leads to a disruption in the protein homeostasis molecular machinery and therefore be lethal for the parasite. While plants are considered excellent sources of bioactive compounds exhibiting inhibition activity towards Pk-ClpP, many local medicinal plants remain unexplored. This article expands the data collected from the inhibition properties of the methanolic extract of Asystasia gangetica (Chinese Violet), Alstonia scholaris (Pulai Tree), Piper retrofractum (Javanese Long Pepper) and Smallanthus sonchifolius (Yacon) towards Pk-ClpP. These plants are widely found in Malaysia and Indonesia and have been traditionally used in various medical treatments. The present dataset showed that the extracts contained phenolic and flavonoid compounds in various concentrations, whereby S. sonchifolius was found to have the lowest content of phenolic and flavonoid contents, while A. gangetica and A. scholaris were statistically comparable, yet higher than P. retrofactum and S. sonchifolus. Further inhibition data assay towards Pk-ClpP revealed that A. gangetica, A. scholaris and P. retrofactum demonstrated remarkable inhibition activity with IC50 values of 39.06 ± 1.98, 48.92 ± 1.52, and 87.63 ± 3.55, respectively. However, the inhibition activity of these extracts was significantly lower than a serine protease inhibitor of phenylmethylsulfonyl fluoridenone (PMSF). Meanwhile, S. sonchifolus did not exhibit significant inhibition activity towards Pk-ClpP. In addition, Pk-ClpP was not inhibited by a cysteine protease inhibitor of E64.http://www.sciencedirect.com/science/article/pii/S2352340921008635Plasmodium knowlesiMalariaCaseinolytic proteasePlant extracts |
| spellingShingle | Raimalynah Abd Razak Meiny Suzery Rafida Razali Zarina Amin Ruzaidi Azli Mohd Mokhtar Ping Chin Lee Cahyo Budiman Technical data on the inhibition properties of some medicinal plant extracts towards caseinolytic protease proteolytic subunit of Plasmodium knowlesi Data in Brief Plasmodium knowlesi Malaria Caseinolytic protease Plant extracts |
| title | Technical data on the inhibition properties of some medicinal plant extracts towards caseinolytic protease proteolytic subunit of Plasmodium knowlesi |
| title_full | Technical data on the inhibition properties of some medicinal plant extracts towards caseinolytic protease proteolytic subunit of Plasmodium knowlesi |
| title_fullStr | Technical data on the inhibition properties of some medicinal plant extracts towards caseinolytic protease proteolytic subunit of Plasmodium knowlesi |
| title_full_unstemmed | Technical data on the inhibition properties of some medicinal plant extracts towards caseinolytic protease proteolytic subunit of Plasmodium knowlesi |
| title_short | Technical data on the inhibition properties of some medicinal plant extracts towards caseinolytic protease proteolytic subunit of Plasmodium knowlesi |
| title_sort | technical data on the inhibition properties of some medicinal plant extracts towards caseinolytic protease proteolytic subunit of plasmodium knowlesi |
| topic | Plasmodium knowlesi Malaria Caseinolytic protease Plant extracts |
| url | http://www.sciencedirect.com/science/article/pii/S2352340921008635 |
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