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Insight into the Interaction of Cationic Porphyrin-Anthraquinone Hybrids with Hsp90: In Silico Analysis

Journal of Mathematical and Fundamental Sciences · Vol. 50 No. 3 (2018) · hlm. 303–314

DOI
10.5614/j.math.fund.sci.2018.50.3.6
ISSN
2338-5510, 2337-5760
Terbit
2018-12-21
Penerbit
Directorate for Research and Innovation (DRI) ITB
Bahasa
eng

Abstrak

Heat shock protein 90 (Hsp90) is responsible for the correct folding of many cellular proteins. Several Hsp90 inhibitors have been developed for cancer treatment. The present in silico study aimed to evaluate the potential of several porphyrin derivatives conjugated with anthraquinone groups as Hsp90 inhibitors by using simulation of molecular docking and molecular dynamics. The binding mode of porphyrin hybrids to Hsp90, which was examined by using AutoDock 4.2, showed that all six porphyrin compounds fit well in the binding pocket of Hsp90. The pi-cationic interactions with Lys58 were exclusively observed in the interaction of each porphyrin hybrid. Stabilities of porphyrin-Hsp90 complexes were confirmed by 40-ns MD simulation, which was carried out with the help of AMBER16. Prediction of ligand affinity by using the MM-PBSA method showed that all complexes were energetically favorable as indicated by a negative binding free energy. The predicted affinities of tris−H2PyP−AQ, tris−H2PzP−AQ, bis−H2PzP−AQ, and mono−H2PzP−AQ are better than those of geldanamycin, a known inhibitor of Hsp90, which shows the importance of the electrostatic and van der Waals energies for ligand binding.

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  • Universitas Halu Oleo
  • Bandung Institute of Technology
  • Sunan Kalijaga State Islamic University Yogyakarta
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  • Organisasi berbeda
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Rekan penulisOrganisasiArtikel bersama
Henny KasmawatiUniversitas Halu Oleo7
Yamin YaminUniversitas Halu Oleo5
Suryani SuryaniUniversitas Halu Oleo4
La Ode Muhammad FitrawanUniversitas Halu Oleo4
Nurull HikmahUniversitas Halu Oleo3
Nurramadhani Armada SidaUniversitas Halu Oleo3
Aswani AswaniUniversitas Halu Oleo3
Muhammad ArbaAfiliasi tidak diketahui3
Ari SartinahUniversitas Halu Oleo3
Sunandar IhsanUniversitas Halu Oleo3
La AbaAfiliasi tidak diketahui2
La AbaUniversitas Halu Oleo2
Fahyuddin FahyuddinAfiliasi tidak diketahui2
Abraham RahmanAfiliasi tidak diketahui2
La HarimuAfiliasi tidak diketahui2
Vica AspadiahAfiliasi tidak diketahui2
Asniar PascayantriUniversitas Halu Oleo2
Rina AndriyaniAfiliasi tidak diketahui1
Syahabudin SyahabudinAfiliasi tidak diketahui1
Suryani SuryaniUniversitas Halu Oleo1
Syahbudin SyahbudinUniversitas Halu Oleo1
Nanik HindaryatiningsihUniversitas Halu Oleo1
La Ode NggawuUniversitas Halu Oleo1
Sabarudin SabarudinUniversitas Halu Oleo1
Rifa’atul MahmuddahUniversitas Halu Oleo1
Fifi Nirmala GUniversitas Halu Oleo1
Sari Sukmawati KapotaUniversitas Halu Oleo1
Hasyim AbdillahSunan Kalijaga State Islamic University Yogyakarta1
Jahiddin JahiddinUniversitas Halu Oleo1
Endah RahminingsihAfiliasi tidak diketahui1
Ritawati AsafAfiliasi tidak diketahui1
Jahidin JahidinAfiliasi tidak diketahui1
Makrawati MakrawatiAfiliasi tidak diketahui1
La SarimuAfiliasi tidak diketahui1
Muliatin MuliatinAfiliasi tidak diketahui1

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Sumber metadata: OAI-PMH (metadata jurnal) https://journals.itb.ac.id/index.php/jmfs/oai, pertama di-harvest 9 Nov 2026, terakhir terlihat 9 Nov 2026.
Metadata asli (oai_dc) 
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	<dc:title xml:lang="en-US">Insight into the Interaction of Cationic Porphyrin-Anthraquinone Hybrids with Hsp90: In Silico Analysis</dc:title>
	<dc:creator>Arba, Muhammad</dc:creator>
	<dc:creator>Ruslin, Ruslin</dc:creator>
	<dc:creator>Kartasasmita, Rahmana Emran</dc:creator>
	<dc:creator>Ibrahiim, Slamet</dc:creator>
	<dc:creator>Tjahjono, Daryono Hadi</dc:creator>
	<dc:subject xml:lang="en-US">Hsp90</dc:subject>
	<dc:subject xml:lang="en-US">MM-PBSA</dc:subject>
	<dc:subject xml:lang="en-US">molecular docking</dc:subject>
	<dc:subject xml:lang="en-US">molecular dynamics simulation</dc:subject>
	<dc:subject xml:lang="en-US">porphyrin</dc:subject>
	<dc:description xml:lang="en-US">Heat shock protein 90 (Hsp90) is responsible for the correct folding of many cellular proteins. Several Hsp90 inhibitors have been developed for cancer treatment. The present in silico study aimed to evaluate the potential of several porphyrin derivatives conjugated with anthraquinone groups as Hsp90 inhibitors by using simulation of molecular docking and molecular dynamics. The binding mode of porphyrin hybrids to Hsp90, which was examined by using AutoDock 4.2, showed that all six porphyrin compounds fit well in the binding pocket of Hsp90. The pi-cationic interactions with Lys58 were exclusively observed in the interaction of each porphyrin hybrid. Stabilities of porphyrin-Hsp90 complexes were confirmed by 40-ns MD simulation, which was carried out with the help of AMBER16. Prediction of ligand affinity by using the MM-PBSA method showed that all complexes were energetically favorable as indicated by a negative binding free energy. The predicted affinities of tris−H2PyP−AQ, tris−H2PzP−AQ, bis−H2PzP−AQ, and mono−H2PzP−AQ are better than those of geldanamycin, a known inhibitor of Hsp90, which shows the importance of the electrostatic and van der Waals energies for ligand binding.</dc:description>
	<dc:publisher xml:lang="en-US">Directorate for Research and Innovation (DRI) ITB</dc:publisher>
	<dc:date>2018-12-21</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://journals.itb.ac.id/index.php/jmfs/article/view/6818</dc:identifier>
	<dc:identifier>10.5614/j.math.fund.sci.2018.50.3.6</dc:identifier>
	<dc:source xml:lang="en-US">Journal of Mathematical and Fundamental Sciences; Vol. 50 No. 3 (2018); 303-314</dc:source>
	<dc:source>2338-5510</dc:source>
	<dc:source>2337-5760</dc:source>
	<dc:source>10.5614/j.math.fund.sci.2018.50.3</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>https://journals.itb.ac.id/index.php/jmfs/article/view/6818/3298</dc:relation>
</oai_dc:dc>