Please use this identifier to cite or link to this item: http://repository.ipb.ac.id/handle/123456789/105351
Title: Pengaruh Mutasi Struktur 3D Protein PfDHFR-TS terhadap Pengikatan Kandidat Obat: Kajian Penambatan Molekul
Other Titles: The Effect of PfDHFR-TS 3D Protein Structure Mutations on Binding of Drug Candidates: Molecular Docking Study
Authors: Wahyudi, Setyanto Tri
Kurniati, Mersi
Adzani, Salsabila Putri
Issue Date: 2021
Publisher: IPB University
Abstract: Plasmodium falciparum adalah jenis parasit malaria yang menyerang manusia dengan infeksi paling parah. Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) adalah pasangan enzim yang bertanggung jawab atas infeksi di dalam sel darah manusia. Mutasi double dan quadruple asam amino pada domain protein DHFR menyebabkan resistansi terhadap pyrimethamine dan cycloguanil sebagai antifolat. Penambatan molekul digunakan pada antifolat untuk mengkaji pengaruh mutasi protein PfDHFR. Penambatan molekul digunakan pula pada 137 senyawa aktif tanaman untuk memperoleh senyawa yang memiliki potensi menghambat protein yang belum termutasi (wild-type) dan telah termutasi (mutan). Penambatan molekul menggunakan parameter seperti energi bebas Gibbs, ikatan hidrogen dan interaksi hidrofobik untuk menentukan afinitas pengikatan senyawa aktif pada protein. Enam senyawa aktif yaitu korupensamine a, dihydrousambarensine, cryptoquindoline, lactupicrin, cryptolepicarboline dan artoindonesianin a-2 memiliki pengikatan kuat pada protein wild-type dan mutan PfDHFR.
Plasmodium falciparum is a type of malaria parasite that attacks humans with the most severe infection. Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) is an enzyme pair responsible for infection in human blood cells. Double and quadruple amino acid mutations in the DHFR protein domain cause resistance to pyrimethamine and cycloguanil as antifolates. Molecular docking was carried out on antifolates to study the effect of mutations in the PfDHFR protein. Molecular docking was also carried out on 137 plant active compounds to obtain compounds that have potential to inhibit wild-type and mutant protein. Molecular docking uses parameters such as Gibbs free energy, hydrogen bond and hydrophobic interaction to determine the binding affinity of the active compounds to the protein. Six active compounds such as korupensamine a, dihydrousambarensine, cryptoquindoline, lactupicrin, cryptolepicarboline and artoindonesianin a-2 have strong binding to wild type and mutant PfDHFR protein.
URI: http://repository.ipb.ac.id/handle/123456789/105351
Appears in Collections:UT - Physics

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G74160059_Salsabila Putri Adzani.pdf
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Lampiran.pdf
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