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author Yagolovich, Anne V
Isakova, Alina A
Kukovyakina, Ekaterina V
Zijian, Yuan
Fedulova, Anastasiia S
Avakiants, Arina V
Shaytan, Alexey K
Dolgikh, Dmitry A
Kirpichnikov, Mikhail P
Gasparian, Marine E
author_facet Yagolovich, Anne V
Isakova, Alina A
Kukovyakina, Ekaterina V
Zijian, Yuan
Fedulova, Anastasiia S
Avakiants, Arina V
Shaytan, Alexey K
Dolgikh, Dmitry A
Kirpichnikov, Mikhail P
Gasparian, Marine E
Yagolovich, Anne V
Isakova, Alina A
Kukovyakina, Ekaterina V
Zijian, Yuan
Fedulova, Anastasiia S
Avakiants, Arina V
Shaytan, Alexey K
Dolgikh, Dmitry A
Kirpichnikov, Mikhail P
Gasparian, Marine E
collection PubMed - marine biology
contents Novel Fusion Protein Based on DR5-Specific TRAIL Variant with Enhanced Antitumor Properties. Yagolovich, Anne V Isakova, Alina A Kukovyakina, Ekaterina V Zijian, Yuan Fedulova, Anastasiia S Avakiants, Arina V Shaytan, Alexey K Dolgikh, Dmitry A Kirpichnikov, Mikhail P Gasparian, Marine E Humans Receptors, TNF-Related Apoptosis-Inducing Ligand Recombinant Fusion Proteins TNF-Related Apoptosis-Inducing Ligand Antineoplastic Agents Vascular Endothelial Growth Factor Receptor-2 Apoptosis Receptor, Fibroblast Growth Factor, Type 1 Cell Line, Tumor The cytokine TRAIL is distinguished by its remarkable ability to preferentially induce apoptosis in transformed, but not in normal, cells. The recombinant TRAIL extracellular domain and other first-generation agonists of DR4 and DR5 death receptors (DRs) have shown very limited antitumor activity in clinical trials. To enhance the antitumor effect, we developed the multitarget recombinant fusion protein SRH-DR5-B-p48 based on the DR5-selective TRAIL variant DR5-B to simultaneously affect tumor cells (DR5-B-mediated apoptosis) and tumor microenvironment, in particular, to suppress angiogenesis. For this purpose, we modeled and produced the recombinant SRH-DR5-B-p48 fusion protein containing antagonistic synthetic peptides (SRH and p48) to VEGFR2 and FGFR1 receptors, respectively. Analysis of molecular trajectories using molecular dynamics methods showed that the SRH and p48 peptides form non-specific temporary contacts with the DR5-B domain. Using enzyme-linked immunosorbent assay, we showed that SRH-DR5-B-p48 was similar to DR5-B in its affinity for the death receptor DR5 and demonstrated a high affinity for VEGFR2 and FGFR1 with nanomolar dissociation constants. SRH-DR5-B-p48 killed tumor cells of various origin more efficiently than DR5-B and destroyed tumor-like structures in 3D cell models, as well as inhibited FGF2-mediated stimulation of fibroblast proliferation. Therefore, the SRH-DR5-B-p48 fusion protein can be considered as a promising agent for the therapy of solid tumors of various origin.
format Artículo científico
id pubmed_41067739
institution PubMed
language en
publishDate 2025
publisher Biochemistry. Biokhimiia
record_format pubmed
spellingShingle Novel Fusion Protein Based on DR5-Specific TRAIL Variant with Enhanced Antitumor Properties.
Yagolovich, Anne V
Isakova, Alina A
Kukovyakina, Ekaterina V
Zijian, Yuan
Fedulova, Anastasiia S
Avakiants, Arina V
Shaytan, Alexey K
Dolgikh, Dmitry A
Kirpichnikov, Mikhail P
Gasparian, Marine E
Humans
Receptors, TNF-Related Apoptosis-Inducing Ligand
Recombinant Fusion Proteins
TNF-Related Apoptosis-Inducing Ligand
Antineoplastic Agents
Vascular Endothelial Growth Factor Receptor-2
Apoptosis
Receptor, Fibroblast Growth Factor, Type 1
Cell Line, Tumor
Novel Fusion Protein Based on DR5-Specific TRAIL Variant with Enhanced Antitumor Properties. Yagolovich, Anne V Isakova, Alina A Kukovyakina, Ekaterina V Zijian, Yuan Fedulova, Anastasiia S Avakiants, Arina V Shaytan, Alexey K Dolgikh, Dmitry A Kirpichnikov, Mikhail P Gasparian, Marine E Humans Receptors, TNF-Related Apoptosis-Inducing Ligand Recombinant Fusion Proteins TNF-Related Apoptosis-Inducing Ligand Antineoplastic Agents Vascular Endothelial Growth Factor Receptor-2 Apoptosis Receptor, Fibroblast Growth Factor, Type 1 Cell Line, Tumor The cytokine TRAIL is distinguished by its remarkable ability to preferentially induce apoptosis in transformed, but not in normal, cells. The recombinant TRAIL extracellular domain and other first-generation agonists of DR4 and DR5 death receptors (DRs) have shown very limited antitumor activity in clinical trials. To enhance the antitumor effect, we developed the multitarget recombinant fusion protein SRH-DR5-B-p48 based on the DR5-selective TRAIL variant DR5-B to simultaneously affect tumor cells (DR5-B-mediated apoptosis) and tumor microenvironment, in particular, to suppress angiogenesis. For this purpose, we modeled and produced the recombinant SRH-DR5-B-p48 fusion protein containing antagonistic synthetic peptides (SRH and p48) to VEGFR2 and FGFR1 receptors, respectively. Analysis of molecular trajectories using molecular dynamics methods showed that the SRH and p48 peptides form non-specific temporary contacts with the DR5-B domain. Using enzyme-linked immunosorbent assay, we showed that SRH-DR5-B-p48 was similar to DR5-B in its affinity for the death receptor DR5 and demonstrated a high affinity for VEGFR2 and FGFR1 with nanomolar dissociation constants. SRH-DR5-B-p48 killed tumor cells of various origin more efficiently than DR5-B and destroyed tumor-like structures in 3D cell models, as well as inhibited FGF2-mediated stimulation of fibroblast proliferation. Therefore, the SRH-DR5-B-p48 fusion protein can be considered as a promising agent for the therapy of solid tumors of various origin.
title Novel Fusion Protein Based on DR5-Specific TRAIL Variant with Enhanced Antitumor Properties.
topic Humans
Receptors, TNF-Related Apoptosis-Inducing Ligand
Recombinant Fusion Proteins
TNF-Related Apoptosis-Inducing Ligand
Antineoplastic Agents
Vascular Endothelial Growth Factor Receptor-2
Apoptosis
Receptor, Fibroblast Growth Factor, Type 1
Cell Line, Tumor
url https://pubmed.ncbi.nlm.nih.gov/41067739/