HANIFA FAUZIYAH, - (2019) DESAIN STRUKTUR MUTAN TOKSIN DIFTERI SECARA IN SILICO SEBAGAI KOMPONEN VAKSIN YANG AMAN DAN IMUNOGENIK. Skripsi thesis, Sekolah Tinggi Farmasi Indonesia.
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Abstract
Difteri merupakan penyakit pernapasan menular yang menjadi salah satu penyebab utama kematian pada anak-anak. Penggunaan formaldehid pada pembuatan toksoid difteri dinilai merusak sejumlah situs antigenik penting pada toksoid. CRM197 merupakan komponen vaksin hasil mutasi asam amino pada toksin difteri. Adanya efek sitotoksisitas CRM197 terhadap sel mamalia dan sel ragi menandakan bahwa mutasi yang dilakukan belum menurunkan toksisitas secara optimal, sehingga diperlukan studi lebih lanjut untuk pengembangan mutan toksin difteri baru. Penelitian ini bertujuan untuk memodelkan mutan tersebut dan menguji afinitasnya terhadap ligan NAD+. Pendekatan bioinformatika dilakukan dengan molecular docking pada AutoDock 4.2. Diperoleh energi bebas ikatan terendah pada kontrol sebesar -7,62 kcal/mol dan RMSD sebesar 1,55. Asam amino Ile31 dan Tyr65, dimutasi menjadi Lys31 dan Gln65 (I31K/Y65Q). Hasil molecular docking mutan uji menunjukkan nilai energi ikatan meningkat menjadi -5,91 kcal/mol, menandakan adanya penurunan afinitas NAD+. Titik mutasi di posisi residu 31 dan 65 serta asam amino pengganti Lys31 dan Gln65 dapat diusulkan dalam pengembangan mutan toksin difteri dengan afinitas rendah terhadap NAD+ sebagai kandidat vaksin difteri.;---Diphtheria is a contagious respiratory disease which is one of the main causes of death in children. The use of formaldehyde in diphtheria toxoid manufacturing was considered to damage a number of important antigenic sites in toxoids. CRM197 is a component of vaccine made from amino acid mutations G52E in diphtheria toxin. The presence of the cytotoxicity effect of CRM197 on mammalian cells and yeast cells indicates that the mutations carried out have not reduced toxicity optimally, so further studies for development of a new diphtheria toxin mutan are needed. This study aims to model the mutant and test its affinity to NAD+ ligand. Bioinformatics approaches are carried out by molecular docking on AutoDock 4.2. The lowest free energy of binding obtained in the control was -7.62 kcal/mol and RMSD of 1.55. Amino acids Ile31 and Tyr65, were mutated to Lys31 and Gln65 (I31K/Y65Q). Molecular docking results showed that the binding energy value increased to -5.91 kcal/mol, indicating a decrease in the affinity of NAD+. Mutation points at residues 31 and 65 with amino acids substitute to Lys31 and Gln65 can be used in the development of diphtheria toxin with low affinity for NAD+ as a candidate for diphtheria vaccine.
| Item Type: | Thesis (Skripsi) |
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| Uncontrolled Keywords: | toksin difteri, Nicotinamide Adenine Dinucleotide (NAD+), mutasi asam amino, molecular docking, vaksin, diphtheria toxin, Nicotinamide Adenine Dinucleotide (NAD+), amino acid mutation, molecular docking, vaccine |
| Subjects: | Q Science > QR Microbiology > QR180 Immunology R Medicine > RS Pharmacy and materia medica |
| Divisions: | Program Studi S1 Farmasi |
| Depositing User: | pustakawan - - |
| Date Deposited: | 19 Sep 2019 10:52 |
| Last Modified: | 05 Jun 2024 07:35 |
| URI: | http://repository.stfi.ac.id/id/eprint/42 |
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