Journal of Pharmacy And Bioallied Sciences
Journal of Pharmacy And Bioallied Sciences Login  | Users Online: 476  Print this pageEmail this pageSmall font sizeDefault font sizeIncrease font size 
    Home | About us | Editorial board | Search | Ahead of print | Current Issue | Past Issues | Instructions | Online submission


ORIGINAL ARTICLE
Year : 2012  |  Volume : 4  |  Issue : 1  |  Page : 56-59

In silico study of fucoxanthin as a tumor cytotoxic agent


Indonesian Research Center for Marine and Fisheries Products Processing and Biotechnology, Jl. KS Tubun Petamburan VI, Slipi - Jakarta Pusat, Indonesia

Correspondence Address:
Hedi I Januar
Indonesian Research Center for Marine and Fisheries Products Processing and Biotechnology, Jl. KS Tubun Petamburan VI, Slipi - Jakarta Pusat
Indonesia
Login to access the Email id

Source of Support: Indonesian Research Center of Marine and Fisheries Products Processing and Biotechnology, Conflict of Interest: None


DOI: 10.4103/0975-7406.92733

Rights and Permissions

Background: Fucoxanthin is a potential tumor cytotoxic compound. However, mechanisms underlying the activities are unclear. Aim: This in silico study aimed to predict the main mechanism of fucoxanthin; whether with its binding to p53 gene, CDK2, or tubulin. Materials and Methods: In silico was studied by using Autodock-Vina's algorithms. The mechanisms being analyzed by comparison of fucoxanthin and native ligands binding energies in p53 gene (1RV1), CDK2 (1AQ1), and three binding sites of tubulin (1JFF-paclitaxel, 1SA0-colchicine, and 1Z2B-vinblastine site). Results: Autodock-Vina's algorithms were valid, as re-docking the native ligands to their receptors showed a RSMD value less than 2 A with binding energies of -11.5 (1RV1), -14.4 (1AQ1), -15.4 (1JFF), -9.2 (1SA0), and -9.7 (1Z2B) kcal/mol. Docking of fucoxanthin to subjected receptors were -6.2 (1RV1), -9.3 (1AQ1), -8.1 (1JFF), -9.2 (1SA0), and -7.2 (1Z2B) kcal/mol. Virtual analysis of fucoxanthin and tubulin binding structure showed the carboxyl moiety in fucoxanthin make a hydrogen bound with 355Val (2.61 A) and 354Ala (2.79 A) at tubulin. Conclusion: The results showed that binding energy of fucoxanthin could only reach the same level as with colchicine ligand in tubulin. Therefore, it may predict that the most probable fucoxanthin main mechanism is to bind tubulin, which causes microtubules depolimerization and cell cycle arrest.


[FULL TEXT] [PDF]*
Print this article     Email this article
 Next article
 Previous article
 Table of Contents

 Similar in PUBMED
   Search Pubmed for
   Search in Google Scholar for
 Related articles
 Citation Manager
 Access Statistics
 Reader Comments
 Email Alert *
 Add to My List *
 * Requires registration (Free)
 

 Article Access Statistics
    Viewed1982    
    Printed103    
    Emailed0    
    PDF Downloaded144    
    Comments [Add]    
    Cited by others 9    

Recommend this journal