Identification of Proteins from Selected Medicinal Plants with Potential Anticancer Properties
Cancer is one of the most feared diseases in the world and is the second leading cause of ath worldwide. With the progression of modern technology, there is an upsurge in the use of natural resources as a direct medicine for cancer treatment. Combining the focus towards the use of natural resource f...
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| Main Author: | |
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| Format: | Thesis |
| Language: | English |
| Published: |
2019
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| Subjects: | |
| Online Access: | http://ir.unimas.my/id/eprint/25225/3/Nurhazlin.pdf |
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| Summary: | Cancer is one of the most feared diseases in the world and is the second leading cause of ath worldwide. With the progression of modern technology, there is an upsurge in the use of natural resources as a direct medicine for cancer treatment. Combining the focus towards the use of natural resource for cancer medicine and the developing interest on peptides as the anticancer agent has led to this research study. The aim of the study was to discover
proteins possessing potential anticancer activity from locally used medicinal plants. Several common plants that traditionally known to have medicinal properties which are Orthosiphon aristatus, Gynura procumbens, Clinacanthus nutans, Piper sarmentosum, Piper betle and
Senna alata were used as the source samples. The crude protein extracts for these plants were extracted overnight by using two buffers; Phosphate Buffered Saline (PBS) and HEPES buffer. Protein profiling and quantification were performed by using SDS-PAGE and
Bradford assay respectively. Nasopharyngeal cell lines (NP-69; normal cell line and HK-1; cancer cell line) were used to test the crude protein extracts for anticancer activity, resultedin narrowing down the targeted plant to Orthosiphon aristatus and Piper sarmentosum. The
two plants samples were fractionized using ammonium sulfate precipitation technique and the fractionized sample cell toxicity values were measured by using MTT assay. The active fractions from both plants sample were identified using LC-MS/MS spectrometry resulted
on a list of identified proteins. |
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