Marine Compounds Screening for Mortalin-p53 binding Inhibitor with Potential as Anti-Cancer
| Main Authors: | Wargasetia, Teresa L., Widodo, Nashi |
|---|---|
| Format: | Proceeding PeerReviewed Book |
| Terbitan: |
, 2017
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| Subjects: | |
| Online Access: |
http://repository.maranatha.edu/24982/1/Update_ECMNP%202017%20%2B%20poster.pdf http://repository.maranatha.edu/24982/ |
| ctrlnum |
24982 |
|---|---|
| fullrecord |
<?xml version="1.0"?>
<dc schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd"><title>Marine Compounds Screening for Mortalin-p53 binding Inhibitor with Potential as Anti-Cancer</title><creator>Wargasetia, Teresa L.</creator><creator>Widodo, Nashi</creator><subject>R Medicine (General)</subject><description>Cancer is the second leading cause of death worldwide. High toxicity and side-effects of some cancer chemotherapy drugs increase the demand for new anti-cancer drugs from natural products. In recent years, attention has been devoted to searching for anti-cancer agents from marine natural products. Mortalin/mtHsp70, a stress response protein, has been reported to contribute to the process of carcinogenesis by several ways including inhibition of the transcriptional activation of p53. In this study, we used computational molecular docking as a tool to find compounds that have potential as anti-cancer by inhibiting the binding between mortalin and p53. 
Marine compounds data was taken from the nuBBE database. To know the anti-cancer potential of the compounds from the database, docking mortalin to the p53 binding domain of the compounds were performed using the Vinaautodock algorithm with pyrx software. The potential inhibition of the binding of mortalin with p53 by the active compounds were analyzed by affinity binding between mortalin and the p53 binding domain of active compound ligands, also by a similarity between the position of mortalin-active compound ligand bindings with mortalin-withanone binding as a positive control. Proteins were visualized with discorystudio software. 
</description><date>2017-09-03</date><type>Journal:Proceeding</type><type>PeerReview:PeerReviewed</type><type>Book:Book</type><identifier>http://repository.maranatha.edu/24982/1/Update_ECMNP%202017%20%2B%20poster.pdf</identifier><identifier> Wargasetia, Teresa L. and Widodo, Nashi (2017) Marine Compounds Screening for Mortalin-p53 binding Inhibitor with Potential as Anti-Cancer. In: 10th European Conference on Marine Natural Products, September 3-7, 2017, Crete. </identifier><relation>http://repository.maranatha.edu/24982/</relation><recordID>24982</recordID></dc>
|
| format |
Journal:Proceeding Journal PeerReview:PeerReviewed PeerReview Book:Book Book |
| author |
Wargasetia, Teresa L. Widodo, Nashi |
| title |
Marine Compounds Screening for Mortalin-p53 binding Inhibitor with Potential as Anti-Cancer |
| publishDate |
2017 |
| topic |
R Medicine (General) |
| url |
http://repository.maranatha.edu/24982/1/Update_ECMNP%202017%20%2B%20poster.pdf http://repository.maranatha.edu/24982/ |
| contents |
Cancer is the second leading cause of death worldwide. High toxicity and side-effects of some cancer chemotherapy drugs increase the demand for new anti-cancer drugs from natural products. In recent years, attention has been devoted to searching for anti-cancer agents from marine natural products. Mortalin/mtHsp70, a stress response protein, has been reported to contribute to the process of carcinogenesis by several ways including inhibition of the transcriptional activation of p53. In this study, we used computational molecular docking as a tool to find compounds that have potential as anti-cancer by inhibiting the binding between mortalin and p53.
Marine compounds data was taken from the nuBBE database. To know the anti-cancer potential of the compounds from the database, docking mortalin to the p53 binding domain of the compounds were performed using the Vinaautodock algorithm with pyrx software. The potential inhibition of the binding of mortalin with p53 by the active compounds were analyzed by affinity binding between mortalin and the p53 binding domain of active compound ligands, also by a similarity between the position of mortalin-active compound ligand bindings with mortalin-withanone binding as a positive control. Proteins were visualized with discorystudio software.
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IOS3452.24982 |
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Universitas Kristen Maranatha |
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45 |
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Perpustakaan Universitas Kristen Maranatha |
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Maranatha Repository System |
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Ekonomi Kesehatan dan Kedokteran Program Komputer dan Teknologi Informasi |
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BANDUNG |
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JAWA BARAT |
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IOS3452 |
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2019-05-06T01:01:28Z |
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2019-05-06T01:01:28Z |
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1685954301248143360 |
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17.60897 |