Figure 3. Red Cicle: The bond between allicin and Tubulin β-chain protein P. falciparum From the picture above, we can see clearly that Allicin can bind to P. falciparum Tubulin β-chain protein protein so that it may influence the protein. Seen from its sequences, allicin has to bind with the active site of protein. The active sites of protein which bonded with allicin are Alanin 206. We can see the bonds molecularly from the picture above.
Figure 3. Molecular Analysis of The Bonds between Allicin and Tubulin β-chain protein Protein P. falciparum
Seen from the Figure above, Allicin binds to Alanin 206 active site through Alkyl bond. The alkyl group has strong bonding with molecule because it releases electrons to carbon, bearing positive charge and thus stabilizes the ion. Increasing the number of bonds adjacent to the carbocation by increasing the number of alkyl groups attached to the carbocation carbon results in an increase in carbocation stability.( Young, 2011). As a result of inhibiting Plasmodium falciparum microtubule sequence( Tubulin β-chain protein), Allicin will prevent the formation of microtubule thread spindle and inhibit the cell proliferation in Plasmodium falciparum.
3.2 Research Findings
The initial search that was conducted yielded a total of 46 trials. After reading the titles, 40 results were excluded as they did not fulfill the inclusion criteria, and a further 2 trials were excluded after reading the abstract. From the resulting 4 texts, 1 did not have a full available article. Thus, a total of 3 resulting trials were used. This information can be seen in the flow chart below:
Initial Search n = n = 46 46
Trial For Which Title were read n = 46 46
Trial For Which Abstract Abstract were readwere n = 6 read n = 6
Trial For Which Full Paper were read n = 4
Trial Excluded after reading the title n = 40
Trial Excluded after reading the Abstract n = 2
Trial Included in This Review n = 3