Melola Discovery

← Melola Discovery

Akses terbuka Jurnal SINTA 1

Chrysin Inhibits Indonesian Serotype Foot-and-Mouth-Disease Virus Replication: Insights from DFT, Molecular Docking and Dynamics Analyses

Journal of Tropical Biodiversity and Biotechnology · Vol. 9 No. 1 (2024)

DOI
10.22146/jtbb.83140
ISSN
2540-9581, 2540-9573
Terbit
2024-01-08
Penerbit
Universitas Gadjah Mada
Bahasa
eng
Lisensi
creativecommons.org/licenses/by-sa/4.0

Abstrak

Chrysin, a predominant compound in Propolis, possesses diverse bioactivities, including antiviral properties. However, its antiviral efficacy against the Indonesian Foot-and-Mouth Disease Virus (FMDV) serotype remains unexplored. This study investigates Chrysin's inhibitory potential against FMDV Indonesian serotype by targeting the 3C Protease (3CP), a vital enzyme for viral replication. Multiple sequence alignment was used to reveal unique characteristics of the Indonesian serotype's 3CP compared to global serotypes. Density Functional Theory (DFT) calculations assessed Chrysin's interaction with 3CP based on electronegativity. Molecular docking and molecular dynamics analyses evaluated Chrysin's inhibitory activity against 3CP, using homology modeling for the Indonesian serotype's 3CP structure. Luteolin, a known FMDV 3CP inhibitor with a similar structure to Chrysin, served as a reference. Results showed distinct 3CP sequences in the Indonesian serotype compared to O serotypes and others. Chrysin exhibited potential electron-donor activity with lower HOMO and LUMO values than Luteolin, but they had similar energy gaps, i.e., 4.016 and 4.044 eV, respectively. Molecular docking indicated similar binding affinities, with Chrysin (-6.365 kcal/mol) and Luteolin (-6.864 kcal/mol) bound to active site residues. Molecular dynamics analysis demonstrated stable 3CP-Chrysin and 3CP-Luteolin complexes, with minor differences in Radius of gyration (Rg) and Root-Mean-Square Fluctuation (RMSF) below 1 Å. From the ligand stability point of view, Chrysin had comparable stability with Luteolin. However, Chrysin formed fewer hydrogen bonds and displayed greater free-binding energy than Luteolin during simulation periods. These findings suggest that Chrysin holds promise as an inhibitor of the Indonesian serotype's FMDV 3C Protease.

Kata kunci

Jaringan kolaborasi para penulis

40 penulis · 114 tautan kepenulisan bersama · 48 lintas organisasi · menampilkan 40 yang paling banyak terhubung

Arahkan kursor atau ketuk sebuah nama untuk menyorot rekan penulisnya. Klik dua kali untuk membuka halaman penulis.

  • University of Brawijaya
  • Shahjalal University of Science and Technology
  • Poltekkes Kemenkes Kendari
  • State University of Makassar
  • Universitas Halu Oleo
  • Universitas Islam Negeri Sumatera Utara
  • Universitas Muhammadiyah Malang
  • Organisasi lain
  • Organisasi berbeda
  • Organisasi sama
  • Afiliasi tidak diketahui
  • Garis lebih tebal = lebih banyak artikel bersama · lingkaran lebih besar = lebih banyak artikel
Tampilkan sebagai tabel
Rekan penulisOrganisasiArtikel bersama
Solimun SolimunUniversity of Brawijaya3
Taamu TaamuPoltekkes Kemenkes Kendari2
Abd. Syukur BauPoltekkes Kemenkes Kendari2
La BanudiPoltekkes Kemenkes Kendari2
Tutut Indria PermanaUniversitas Muhammadiyah Malang2
Rahman RahmanUniversitas Halu Oleo1
Silvy Kusmiranty NurUniversitas Halu Oleo1
M. Fikar PapaliaUniversity of Brawijaya1
Rindu HardiantiUniversity of Brawijaya1
Ni Wayan Surya WardhaniUniversity of Brawijaya1
Adji Achmad Rinaldo FernandesUniversity of Brawijaya1
Yossy Maynaldi PratamaUniversity of Brawijaya1
Suci AstutikUniversity of Brawijaya1
Darmanto DarmantoSebelas Maret University1
Diego IrsandyUniversity of Brawijaya1
İsnani DartiUniversity of Brawijaya1
Muhammad Hisyam LeeUniversity of Technology Malaysia1
Rismania Hartanti Putri Yulianing DamayantiUniversity of Brawijaya1
Rima ApriliaUniversitas Islam Negeri Sumatera Utara1
Hendra CiptaUniversitas Islam Negeri Sumatera Utara1
Nurdiana NurdianaState University of Makassar1
Muhammad HasanState University of Makassar1
Kurniawati KurniawatiIndonesia University of Education1
Andi Caezar To TadampaliState University of Makassar1
Depison DepisonUniversitas Jambi1
Md. Khyrul Alam TalukderShahjalal University of Science and Technology1
Md. Murad HossainShahjalal University of Science and Technology1
Wahidu ZzamanShahjalal University of Science and Technology1
Mahmudul Hasan MithunShahjalal University of Science and Technology1
Md. Nazmul IslamShahjalal University of Science and Technology1
Tanjir HosenShahjalal University of Science and Technology1
Nurul HudaUniversity of Brawijaya1
Rahmadeni RahmadeniUniversitas Islam Negeri Sultan Syarif Kasim Riau1
M. Rifqinizamy KarsayudaLambung Mangkurat University1

Afiliasi berasal dari OpenAlex; metadata OAI-PMH jurnal tidak memuatnya. Penulis tanpa ID OpenAlex dicocokkan berdasarkan nama, sehingga dua orang bisa tergabung atau satu orang bisa terpisah.

Sumber metadata: OAI-PMH (metadata jurnal) https://jurnal.ugm.ac.id/jtbb/oai, pertama di-harvest 9 Nov 2026, terakhir terlihat 9 Nov 2026.
Metadata asli (oai_dc) 
<oai_dc:dc xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/  http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
	<dc:title xml:lang="en-US">Chrysin Inhibits Indonesian Serotype Foot-and-Mouth-Disease Virus Replication: Insights from DFT, Molecular Docking and Dynamics Analyses</dc:title>
	<dc:creator>Susilo, Agus</dc:creator>
	<dc:creator>Cahyati, Miftakhul</dc:creator>
	<dc:creator>Nurjannah, Nurjannah</dc:creator>
	<dc:creator>Pranowo, Dodyk</dc:creator>
	<dc:creator>Hermanto, Feri Eko</dc:creator>
	<dc:creator>Primandasari, Elma Putri</dc:creator>
	<dc:subject xml:lang="en-US"></dc:subject>
	<dc:subject xml:lang="en-US">3C Protease; antivirus; Chrysin; Foot-and-Mouth-Disease Virus; Propolis.</dc:subject>
	<dc:description xml:lang="en-US">Chrysin, a predominant compound in Propolis, possesses diverse bioactivities, including antiviral properties. However, its antiviral efficacy against the Indonesian Foot-and-Mouth Disease Virus (FMDV) serotype remains unexplored. This study investigates Chrysin's inhibitory potential against FMDV Indonesian serotype by targeting the 3C Protease (3CP), a vital enzyme for viral replication. Multiple sequence alignment was used to reveal unique characteristics of the Indonesian serotype's 3CP compared to global serotypes. Density Functional Theory (DFT) calculations assessed Chrysin's interaction with 3CP based on electronegativity. Molecular docking and molecular dynamics analyses evaluated Chrysin's inhibitory activity against 3CP, using homology modeling for the Indonesian serotype's 3CP structure. Luteolin, a known FMDV 3CP inhibitor with a similar structure to Chrysin, served as a reference. Results showed distinct 3CP sequences in the Indonesian serotype compared to O serotypes and others. Chrysin exhibited potential electron-donor activity with lower HOMO and LUMO values than Luteolin, but they had similar energy gaps, i.e., 4.016 and 4.044 eV, respectively. Molecular docking indicated similar binding affinities, with Chrysin (-6.365 kcal/mol) and Luteolin (-6.864 kcal/mol) bound to active site residues. Molecular dynamics analysis demonstrated stable 3CP-Chrysin and 3CP-Luteolin complexes, with minor differences in Radius of gyration (Rg) and Root-Mean-Square Fluctuation (RMSF) below 1 Å. From the ligand stability point of view, Chrysin had comparable stability with Luteolin. However, Chrysin formed fewer hydrogen bonds and displayed greater free-binding energy than Luteolin during simulation periods. These findings suggest that Chrysin holds promise as an inhibitor of the Indonesian serotype's FMDV 3C Protease. </dc:description>
	<dc:publisher xml:lang="en-US">Universitas Gadjah Mada</dc:publisher>
	<dc:contributor xml:lang="en-US">Prof. Nashi Widodo, Ph.D.Med.Sc.</dc:contributor>
	<dc:contributor xml:lang="en-US">Brawijaya University</dc:contributor>
	<dc:date>2024-01-08</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:type xml:lang="en-US"></dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://journal.ugm.ac.id/jtbb/article/view/83140</dc:identifier>
	<dc:identifier>10.22146/jtbb.83140</dc:identifier>
	<dc:source xml:lang="en-US">Journal of Tropical Biodiversity and Biotechnology; Vol 9, No 1 (2024): March; jtbb83140</dc:source>
	<dc:source>2540-9581</dc:source>
	<dc:source>2540-9573</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>https://journal.ugm.ac.id/jtbb/article/view/83140/37620</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/jtbb/article/downloadSuppFile/83140/25932</dc:relation>
	<dc:relation>https://journal.ugm.ac.id/jtbb/article/downloadSuppFile/83140/25933</dc:relation>
	<dc:coverage xml:lang="en-US"></dc:coverage>
	<dc:coverage xml:lang="en-US"></dc:coverage>
	<dc:coverage xml:lang="en-US"></dc:coverage>
	<dc:rights xml:lang="en-US">Copyright (c) 2024 Journal of Tropical Biodiversity and Biotechnology</dc:rights>
	<dc:rights xml:lang="en-US">http://creativecommons.org/licenses/by-sa/4.0</dc:rights>
</oai_dc:dc>