Penambatan Molekuler α, β, dan γ-mangostin Sebagai Inhibitor α-amilase Pankreas Manusia
In silico studies on interactions between the human pancreatic α-amylase (HPA) enzyme with α, β, and γ-mangostin ligands has been carried out using the molecular docking method. Ligands α, β, and γ-mangostin interact through the formation of hydrogen and van der waals bonds with residues on the enzy...
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| Format: | Article |
| Language: | English |
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Department of Chemistry, Pattimura University
2019-01-01
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| Series: | Indonesian Journal of Chemical Research |
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| Online Access: | https://ojs3.unpatti.ac.id/index.php/ijcr/article/view/699 |
| _version_ | 1818789047980523520 |
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| author | Nelson Gaspersz Mario Rowan Sohilait |
| author_facet | Nelson Gaspersz Mario Rowan Sohilait |
| author_sort | Nelson Gaspersz |
| collection | DOAJ |
| description | In silico studies on interactions between the human pancreatic α-amylase (HPA) enzyme with α, β, and γ-mangostin ligands has been carried out using the molecular docking method. Ligands α, β, and γ-mangostin interact through the formation of hydrogen and van der waals bonds with residues on the enzyme active side. The α-mangostin ligands form seven hydrogen and six van der waals bonds with residues involved were Trp59, Gln63, Trp96, Thr163, Thr164, Ala198, His201, Glu233, and Asp300; β-mangostin forms five hydrogen and eight van der waals bonds with residues involved were Gln63, Trp96, Thr163, Thr164, Arg195, Asp197, His201, Glu233, Asp300, and His305; while γ-mangostin forms nine hydrogen and five van der waals bonds with residues involved were Trp59, Gln63, Trp96, Thr163, Asp197, Ala198, His201, Glu233, and Asp300. The binding afinity of α, β, and γ-mangostin to the HPA obtained were -7.0; -6.6; and -7.4 kcal/mol with RMSD value were 1,850; 1,956; and 1,811 Å, respectively. The number of hydrogen bonds that can be formed was responsible to the binding affinity. Ligand γ-mangostin has potential activity as an inhibitor of HPA enzyme due to the stable complexes formation with lower binding affinity (validated with RMSD value) when compared to α and β-mangostin. |
| first_indexed | 2024-12-18T14:33:22Z |
| format | Article |
| id | doaj.art-394f1d1b207d471a88bd96022b4ed369 |
| institution | Directory Open Access Journal |
| issn | 2338-5359 2614-2627 |
| language | English |
| last_indexed | 2024-12-18T14:33:22Z |
| publishDate | 2019-01-01 |
| publisher | Department of Chemistry, Pattimura University |
| record_format | Article |
| series | Indonesian Journal of Chemical Research |
| spelling | doaj.art-394f1d1b207d471a88bd96022b4ed3692022-12-21T21:04:32ZengDepartment of Chemistry, Pattimura UniversityIndonesian Journal of Chemical Research2338-53592614-26272019-01-016210.30598//ijcr.2019.6-nelPenambatan Molekuler α, β, dan γ-mangostin Sebagai Inhibitor α-amilase Pankreas ManusiaNelson Gaspersz0Mario Rowan Sohilait1Department of Chemistry, Faculty of Matemathic and Natural Sciences, Pattimura University, Ambon 97233Department of Chemistry, Faculty of Matemathic and Natural Sciences, Pattimura University, Ambon 97233In silico studies on interactions between the human pancreatic α-amylase (HPA) enzyme with α, β, and γ-mangostin ligands has been carried out using the molecular docking method. Ligands α, β, and γ-mangostin interact through the formation of hydrogen and van der waals bonds with residues on the enzyme active side. The α-mangostin ligands form seven hydrogen and six van der waals bonds with residues involved were Trp59, Gln63, Trp96, Thr163, Thr164, Ala198, His201, Glu233, and Asp300; β-mangostin forms five hydrogen and eight van der waals bonds with residues involved were Gln63, Trp96, Thr163, Thr164, Arg195, Asp197, His201, Glu233, Asp300, and His305; while γ-mangostin forms nine hydrogen and five van der waals bonds with residues involved were Trp59, Gln63, Trp96, Thr163, Asp197, Ala198, His201, Glu233, and Asp300. The binding afinity of α, β, and γ-mangostin to the HPA obtained were -7.0; -6.6; and -7.4 kcal/mol with RMSD value were 1,850; 1,956; and 1,811 Å, respectively. The number of hydrogen bonds that can be formed was responsible to the binding affinity. Ligand γ-mangostin has potential activity as an inhibitor of HPA enzyme due to the stable complexes formation with lower binding affinity (validated with RMSD value) when compared to α and β-mangostin.https://ojs3.unpatti.ac.id/index.php/ijcr/article/view/699Molecular docking, HPA enzyme, α, β, and γ-mangostin. |
| spellingShingle | Nelson Gaspersz Mario Rowan Sohilait Penambatan Molekuler α, β, dan γ-mangostin Sebagai Inhibitor α-amilase Pankreas Manusia Indonesian Journal of Chemical Research Molecular docking, HPA enzyme, α, β, and γ-mangostin. |
| title | Penambatan Molekuler α, β, dan γ-mangostin Sebagai Inhibitor α-amilase Pankreas Manusia |
| title_full | Penambatan Molekuler α, β, dan γ-mangostin Sebagai Inhibitor α-amilase Pankreas Manusia |
| title_fullStr | Penambatan Molekuler α, β, dan γ-mangostin Sebagai Inhibitor α-amilase Pankreas Manusia |
| title_full_unstemmed | Penambatan Molekuler α, β, dan γ-mangostin Sebagai Inhibitor α-amilase Pankreas Manusia |
| title_short | Penambatan Molekuler α, β, dan γ-mangostin Sebagai Inhibitor α-amilase Pankreas Manusia |
| title_sort | penambatan molekuler α β dan γ mangostin sebagai inhibitor α amilase pankreas manusia |
| topic | Molecular docking, HPA enzyme, α, β, and γ-mangostin. |
| url | https://ojs3.unpatti.ac.id/index.php/ijcr/article/view/699 |
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