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Computational Study of Nocardiotide-A Analogues in the Development of Technetium-99m Radiopeptides for Cancer Imaging for Targeting Somatostatin Receptor 2

Journal of Mathematical and Fundamental Sciences · Vol. 55 No. 1 (2023) · hlm. 77–91

DOI
10.5614/j.math.fund.sci.2023.55.1.5
ISSN
2338-5510, 2337-5760
Terbit
2023-10-07
Penerbit
Directorate for Research and Innovation (DRI) ITB
Bahasa
eng

Abstrak

Nocardiotide-A (cWIWLVA) is a cyclic peptide with significant cytotoxicity against several cancer cells. The present research aimed to design a radiopeptide based on nocardiotide-A analogues to be labeled by technetium-99m targeting SSTR2, which is the most widely expressed receptor in several types of human cancers and used as radiopeptide target. Nocardiotide-A analogues were individually designed by replacing valine at the lead compound with lysine, arginine, histidine, asparagine, and glutamine, and this was simulated by molecular dynamics using AMBER18. A molecular docking using AutoDock 4.2 was performed and evaluated to understand the effect of chelation of technetium-99m on 99mTc-HYNIC-EDDA and 99mTc-HYNIC-tricine on the binding affinity of nocardiotide-A analogues. The molecular dynamics simulation confirmed that the designed nocardiotide-A-based peptides were stable in the binding pocket of SSTR2 for 200 ns. Moreover, the nocardiotide-A-based radiopeptides are able to interact with residues Q102, D122, Q126, and N276 by building hydrogen bonds, which are essential binding residues in SSTR2. The molecular docking simulation revealed that the best docking parameter is exhibited by 99mTc/EDDA/HYNIC-cWIWLNA and 99mTc/tricine/HYNIC-cWIWLNA with a binding free energy of –12.59 kcal/mol and –8.96 kcal/mol, respectively. Taken together, nocardiotide-A-based radiopeptides are prospective to be further developed for cancer imaging targeting SSTR2.

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  • Padjadjaran University
  • Bandung Institute of Technology
  • Universitas Halu Oleo
  • National Nuclear Energy Agency of Indonesia
  • University of Indonesia
  • National Research and Innovation Agency
  • Yamagata University
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Rekan penulisOrganisasiArtikel bersama
Unang SupratmanPadjadjaran University11
Nurlelasari NurlelasariPadjadjaran University10
Kindi FarabiPadjadjaran University9
Desi HarnetiPadjadjaran University8
Tri MayantiPadjadjaran University8
Darwati DarwatiPadjadjaran University5
Yoshihito ShionoYamagata University5
Al Arofatus NainiPadjadjaran University4
Ace Tatang HidayatPadjadjaran University4
Mohamad Nurul AzmiUniversiti Sains Malaysia4
Muhammad ArbaUniversitas Halu Oleo4
Sofa FajriahNational Research and Innovation Agency3
Ruslin RuslinUniversitas Halu Oleo3
Erina HilmayantiPadjadjaran University2
Muhammad HanafiNational Research and Innovation Agency2
Desi Harneti Putri HuspaPadjadjaran University2
Slamet IbrahiimAfiliasi tidak diketahui2
Eva Maria WidyasariNational Nuclear Energy Agency of Indonesia1
Maula Eka SriyaniNational Nuclear Energy Agency of Indonesia1
Esty KusumawardhanyAfiliasi tidak diketahui1
Muharam MarzukiAfiliasi tidak diketahui1
Aiyi AsnawiBandung Institute of Technology1
As’ari NawawiBandung Institute of Technology1
Slamet IbrahimBandung Institute of Technology1
Harmoko HarmokoAfiliasi tidak diketahui1
Astika TresnawatiAfiliasi tidak diketahui1
Tutus GusdinarBandung Institute of Technology1
I Ketut AdnyanaBandung Institute of Technology1
Rina HerowatiUniversitas Setia Budi1
Chusnul ChotimahUniversity of Indonesia1
Muhayatun SantosoNational Nuclear Energy Agency of Indonesia1
Benny S. LatiefUniversity of Indonesia1
Marlia SinggihBandung Institute of Technology1
Arry YanuarUniversity of Indonesia1
Sanang Nur SafitriUniversitas Halu Oleo1
Andry Nur HidayatUniversitas Halu Oleo1

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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">Computational Study of Nocardiotide-A Analogues in the Development of Technetium-99m Radiopeptides for Cancer Imaging for Targeting Somatostatin Receptor 2 </dc:title>
	<dc:creator>Sugiharti, Rizky Juwita</dc:creator>
	<dc:creator>Maharani, Rani</dc:creator>
	<dc:creator>Kartasasmita, Rahmana Emran</dc:creator>
	<dc:creator>Tjahjono, Daryono Hadi</dc:creator>
	<dc:subject xml:lang="en-US">molecular docking</dc:subject>
	<dc:subject xml:lang="en-US">nocardiotide-A</dc:subject>
	<dc:subject xml:lang="en-US">radiopeptide</dc:subject>
	<dc:subject xml:lang="en-US">99mTc</dc:subject>
	<dc:subject xml:lang="en-US">SSTR2</dc:subject>
	<dc:subject xml:lang="en-US">Radiopharmacy</dc:subject>
	<dc:description xml:lang="en-US">Nocardiotide-A (cWIWLVA) is a cyclic peptide with significant cytotoxicity against several cancer cells. The present research aimed to design a radiopeptide based on nocardiotide-A analogues to be labeled by technetium-99m targeting SSTR2, which is the most widely expressed receptor in several types of human cancers and used as radiopeptide target. Nocardiotide-A analogues were individually designed by replacing valine at the lead compound with lysine, arginine, histidine, asparagine, and glutamine, and this was simulated by molecular dynamics using AMBER18. A molecular docking using AutoDock 4.2 was performed and evaluated to understand the effect of chelation of technetium-99m on 99mTc-HYNIC-EDDA and 99mTc-HYNIC-tricine on the binding affinity of nocardiotide-A analogues. The molecular dynamics simulation confirmed that the designed nocardiotide-A-based peptides were stable in the binding pocket of SSTR2 for 200 ns. Moreover, the nocardiotide-A-based radiopeptides are able to interact with residues Q102, D122, Q126, and N276 by building hydrogen bonds, which are essential binding residues in SSTR2. The molecular docking simulation revealed that the best docking parameter is exhibited by 99mTc/EDDA/HYNIC-cWIWLNA and 99mTc/tricine/HYNIC-cWIWLNA with a binding free energy of –12.59 kcal/mol and –8.96 kcal/mol, respectively. Taken together, nocardiotide-A-based radiopeptides are prospective to be further developed for cancer imaging targeting SSTR2.</dc:description>
	<dc:publisher xml:lang="en-US">Directorate for Research and Innovation (DRI) ITB</dc:publisher>
	<dc:date>2023-10-07</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/20259</dc:identifier>
	<dc:identifier>10.5614/j.math.fund.sci.2023.55.1.5</dc:identifier>
	<dc:source xml:lang="en-US">Journal of Mathematical and Fundamental Sciences; Vol. 55 No. 1 (2023); 77-91</dc:source>
	<dc:source>2338-5510</dc:source>
	<dc:source>2337-5760</dc:source>
	<dc:source>10.5614/j.math.fund.sci.2023.55.1</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>https://journals.itb.ac.id/index.php/jmfs/article/view/20259/6351</dc:relation>
	<dc:rights xml:lang="en-US">Copyright (c) 2023 Journal of Mathematical and Fundamental Sciences</dc:rights>
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