Molecular docking analysis of Cinnamomum zeylanicum phytochemicals against Secreted Aspartyl Proteinase 4–6 of Candida albicans as anti-candidiasis oral
Candida albicans is a polymorphic human microflora species, which caused a candidiasis. This disease frequently occurred in immunocompromised patients with considerable medical outcomes due to the damage from its infections. Secreted Aspartic Proteinase (SAP) 4–6 regulated the virulence of C. albica...
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| Format: | Article |
| Language: | English |
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Elsevier
2023-01-01
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| Series: | Results in Chemistry |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211715622004404 |
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| author | Vita Meylani Rinaldi Rizal Putra Muhammad Miftahussurur Sukardiman Sukardiman Feri Eko Hermanto Abdullah Abdullah |
| author_facet | Vita Meylani Rinaldi Rizal Putra Muhammad Miftahussurur Sukardiman Sukardiman Feri Eko Hermanto Abdullah Abdullah |
| author_sort | Vita Meylani |
| collection | DOAJ |
| description | Candida albicans is a polymorphic human microflora species, which caused a candidiasis. This disease frequently occurred in immunocompromised patients with considerable medical outcomes due to the damage from its infections. Secreted Aspartic Proteinase (SAP) 4–6 regulated the virulence of C. albicans. Thus, inhibiting those protenases may useful to obtain a better prognosis. On the other hand, Cinnamomum zeylanicum reported to have anti-cadidiasis. However, the mechanism of action on the anti-cadidiasis activity remains unclear. This study will explain the possible mechanism of anti-candidiasis from the bioactives of C. zeylanicum through SAP 4–6 inhibion. A computational analysis was employed by molecular docking coupled with molecular dynamics simulation to comprehend the interaction among C. zeylanicum bioactives to SAP 4–6. Positive docking outcomes were observed, with Cinnamaldehyde, Pyrantel Hydrochloride, and Hexadecenoic Acidbecame showed promising binding affinity against SAP 4–6. However, those compounds interacted with different residues of each proteinase. Only Hexadenoic Acid bound to the catalytic residues of SAP5-6. Molecular dynamics simulated the stable binding of Hexadecenoid Acid to the SAP5-6. Not only has stable structural integrity, the binding of Hexadecenoic Acidalso showed minimum alterations on the structural stability of SAP5-6, which suggested a stable inhibitory activity. The stable binding of Hexadecenoid Acid also displayed by the prominent number of hydrogen bond and the free-binding energy simulations. In conclusion, the anti-candidiasis activity of C. zeylanicum may take place in the SAP5-6 inhibition, mainly by Hexadecenoic Acid. |
| first_indexed | 2024-03-13T04:14:00Z |
| format | Article |
| id | doaj.art-d8453ae1f8c44f81bc1d36ab2cf1cafa |
| institution | Directory Open Access Journal |
| issn | 2211-7156 |
| language | English |
| last_indexed | 2024-03-13T04:14:00Z |
| publishDate | 2023-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Results in Chemistry |
| spelling | doaj.art-d8453ae1f8c44f81bc1d36ab2cf1cafa2023-06-21T06:51:43ZengElsevierResults in Chemistry2211-71562023-01-015100721Molecular docking analysis of Cinnamomum zeylanicum phytochemicals against Secreted Aspartyl Proteinase 4–6 of Candida albicans as anti-candidiasis oralVita Meylani0Rinaldi Rizal Putra1Muhammad Miftahussurur2Sukardiman Sukardiman3Feri Eko Hermanto4Abdullah Abdullah5Department of Biology Education, Faculty of Education and Teacher Training, Tasikmalaya, West Java, Indonesia; Corresponding author.Department of Biology Education, Faculty of Education and Teacher Training, Tasikmalaya, West Java, IndonesiaDivision of Gastroentero-Hepatology, Department of Internal Medicine, Faculty of Medicine, Universitas Airlangga, Surabaya, East Java, Indonesia; Institute of Tropical Diseases, Universitas Airlangga, Surabaya, East Java, IndonesiaDepartment of Pharmacognosy and Phytochemistry, Faculty of Pharmacy, Universitas Airlangga, Surabaya, East Java, IndonesiaDepartment of Biology, Faculty of Mathematics and Sciences, Universitas Brawijaya, Malang, Indonesia; Bioinformatics Research Center, Indonesian Institute of Bioinformatics (INBIO), Malang, IndonesiaDepartment of Biology, Faculty of Mathematics and Sciences, Universitas Brawijaya, Malang, IndonesiaCandida albicans is a polymorphic human microflora species, which caused a candidiasis. This disease frequently occurred in immunocompromised patients with considerable medical outcomes due to the damage from its infections. Secreted Aspartic Proteinase (SAP) 4–6 regulated the virulence of C. albicans. Thus, inhibiting those protenases may useful to obtain a better prognosis. On the other hand, Cinnamomum zeylanicum reported to have anti-cadidiasis. However, the mechanism of action on the anti-cadidiasis activity remains unclear. This study will explain the possible mechanism of anti-candidiasis from the bioactives of C. zeylanicum through SAP 4–6 inhibion. A computational analysis was employed by molecular docking coupled with molecular dynamics simulation to comprehend the interaction among C. zeylanicum bioactives to SAP 4–6. Positive docking outcomes were observed, with Cinnamaldehyde, Pyrantel Hydrochloride, and Hexadecenoic Acidbecame showed promising binding affinity against SAP 4–6. However, those compounds interacted with different residues of each proteinase. Only Hexadenoic Acid bound to the catalytic residues of SAP5-6. Molecular dynamics simulated the stable binding of Hexadecenoid Acid to the SAP5-6. Not only has stable structural integrity, the binding of Hexadecenoic Acidalso showed minimum alterations on the structural stability of SAP5-6, which suggested a stable inhibitory activity. The stable binding of Hexadecenoid Acid also displayed by the prominent number of hydrogen bond and the free-binding energy simulations. In conclusion, the anti-candidiasis activity of C. zeylanicum may take place in the SAP5-6 inhibition, mainly by Hexadecenoic Acid.http://www.sciencedirect.com/science/article/pii/S2211715622004404Candida albicansSecreted Aspartic Proteinase (SAP)C. zeylanicumPhytochemicalsIn silicoAutoDock |
| spellingShingle | Vita Meylani Rinaldi Rizal Putra Muhammad Miftahussurur Sukardiman Sukardiman Feri Eko Hermanto Abdullah Abdullah Molecular docking analysis of Cinnamomum zeylanicum phytochemicals against Secreted Aspartyl Proteinase 4–6 of Candida albicans as anti-candidiasis oral Results in Chemistry Candida albicans Secreted Aspartic Proteinase (SAP) C. zeylanicum Phytochemicals In silico AutoDock |
| title | Molecular docking analysis of Cinnamomum zeylanicum phytochemicals against Secreted Aspartyl Proteinase 4–6 of Candida albicans as anti-candidiasis oral |
| title_full | Molecular docking analysis of Cinnamomum zeylanicum phytochemicals against Secreted Aspartyl Proteinase 4–6 of Candida albicans as anti-candidiasis oral |
| title_fullStr | Molecular docking analysis of Cinnamomum zeylanicum phytochemicals against Secreted Aspartyl Proteinase 4–6 of Candida albicans as anti-candidiasis oral |
| title_full_unstemmed | Molecular docking analysis of Cinnamomum zeylanicum phytochemicals against Secreted Aspartyl Proteinase 4–6 of Candida albicans as anti-candidiasis oral |
| title_short | Molecular docking analysis of Cinnamomum zeylanicum phytochemicals against Secreted Aspartyl Proteinase 4–6 of Candida albicans as anti-candidiasis oral |
| title_sort | molecular docking analysis of cinnamomum zeylanicum phytochemicals against secreted aspartyl proteinase 4 6 of candida albicans as anti candidiasis oral |
| topic | Candida albicans Secreted Aspartic Proteinase (SAP) C. zeylanicum Phytochemicals In silico AutoDock |
| url | http://www.sciencedirect.com/science/article/pii/S2211715622004404 |
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