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Optimized Heterologous Expression and Efficient Purification of a New TRAIL-Based Antitumor Fusion Protein SRH–DR5-B with Dual VEGFR2 and DR5 Receptor Specificity

Тип публикацииJournal Article
Дата публикации2022-05-24
scimago Q1
wos Q1
БС1
SJR1.273
CiteScore9.0
Impact factor4.9
ISSN16616596, 14220067
Catalysis
Organic Chemistry
Inorganic Chemistry
Physical and Theoretical Chemistry
Computer Science Applications
Spectroscopy
Molecular Biology
General Medicine
Краткое описание

In the last two decades, bifunctional proteins have been created by genetic and protein engineering methods to increase therapeutic effects in various diseases, including cancer. Unlike conventional small molecule or monotargeted drugs, bifunctional proteins have increased biological activity while maintaining low systemic toxicity. The recombinant anti-cancer cytokine TRAIL has shown a limited therapeutic effect in clinical trials. To enhance the efficacy of TRAIL, we designed the HRH–DR5-B fusion protein based on the DR5-selective mutant variant of TRAIL fused to the anti-angiogenic synthetic peptide HRHTKQRHTALH. Initially low expression of HRH–DR5-B was enhanced by the substitution of E. coli-optimized codons with AT-rich codons in the DNA sequence encoding the first 7 amino acid residues of the HRH peptide. However, the HRH–DR5-B degraded during purification to form two adjacent protein bands on the SDS-PAGE gel. The replacement of His by Ser at position P2 immediately after the initiator Met dramatically minimized degradation, allowing more than 20 mg of protein to be obtained from 200 mL of cell culture. The resulting SRH–DR5-B fusion bound the VEGFR2 and DR5 receptors with high affinity and showed increased cytotoxic activity in 3D multicellular tumor spheroids. SRH–DR5-B can be considered as a promising candidate for therapeutic applications.

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International Journal of Molecular Sciences
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Molecular Biotechnology
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International Journal of Biological Macromolecules
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Cancer Medicine
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Russian Chemical Reviews
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Biochemistry (Moscow)
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ГОСТ |
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Yagolovich A. V. et al. Optimized Heterologous Expression and Efficient Purification of a New TRAIL-Based Antitumor Fusion Protein SRH–DR5-B with Dual VEGFR2 and DR5 Receptor Specificity // International Journal of Molecular Sciences. 2022. Vol. 23. No. 11. p. 5860.
ГОСТ со всеми авторами (до 50) Скопировать
Yagolovich A. V., Artykov A., Isakova A. A., Vorontsova Y. V., Dolgikh D. А., Kirpichnikov M. P., Gasparian M. E. Optimized Heterologous Expression and Efficient Purification of a New TRAIL-Based Antitumor Fusion Protein SRH–DR5-B with Dual VEGFR2 and DR5 Receptor Specificity // International Journal of Molecular Sciences. 2022. Vol. 23. No. 11. p. 5860.
RIS |
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TY - JOUR
DO - 10.3390/ijms23115860
UR - https://doi.org/10.3390/ijms23115860
TI - Optimized Heterologous Expression and Efficient Purification of a New TRAIL-Based Antitumor Fusion Protein SRH–DR5-B with Dual VEGFR2 and DR5 Receptor Specificity
T2 - International Journal of Molecular Sciences
AU - Yagolovich, Anne V.
AU - Artykov, Artem
AU - Isakova, Alina A
AU - Vorontsova, Yekaterina V
AU - Dolgikh, D. А.
AU - Kirpichnikov, Mikhail P.
AU - Gasparian, Marine E.
PY - 2022
DA - 2022/05/24
PB - MDPI
SP - 5860
IS - 11
VL - 23
PMID - 35682540
SN - 1661-6596
SN - 1422-0067
ER -
BibTex |
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@article{2022_Yagolovich,
author = {Anne V. Yagolovich and Artem Artykov and Alina A Isakova and Yekaterina V Vorontsova and D. А. Dolgikh and Mikhail P. Kirpichnikov and Marine E. Gasparian},
title = {Optimized Heterologous Expression and Efficient Purification of a New TRAIL-Based Antitumor Fusion Protein SRH–DR5-B with Dual VEGFR2 and DR5 Receptor Specificity},
journal = {International Journal of Molecular Sciences},
year = {2022},
volume = {23},
publisher = {MDPI},
month = {may},
url = {https://doi.org/10.3390/ijms23115860},
number = {11},
pages = {5860},
doi = {10.3390/ijms23115860}
}
MLA
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Yagolovich, Anne V., et al. “Optimized Heterologous Expression and Efficient Purification of a New TRAIL-Based Antitumor Fusion Protein SRH–DR5-B with Dual VEGFR2 and DR5 Receptor Specificity.” International Journal of Molecular Sciences, vol. 23, no. 11, May. 2022, p. 5860. https://doi.org/10.3390/ijms23115860.