The Use of Glycine-Containing Peptide-Based Chelators for Labeling with 99mTc Improves the Imaging Properties of EpCAM-Targeting Designed Ankyrin Repeat Ec1; Molecular Pharmaceutics; Vol. 23, iss. 4

Podrobná bibliografie
Parent link:Molecular Pharmaceutics.— .— Washington: ACS Publications
Vol. 23, iss. 4.— 2026.— P. 2469–2480
Další autoři: Deev S. M. Sergey Mikhaylovich, Fominykh A. S. Anastasiya Sergeevna, Varvashenya R. N. Ruslan Nikolaevich, Yanovich G. Gleb, Bodenko V. V. Vitalina Vasiljevna, Plotnikov E. V. Evgeny Vladimirovich, Tretyakova (Tretjyakova) M. S. Maria Sergeevna, Eskova D. D. Darjya Dmitrievna, Zelchan (Zeltchan) R. V. Roman Vladimirovich, Shulga (Schulga) A. A. Aleksey Anatolievich, Konovalova E. V. Elena Valerjevna, Ziganshin R. Rustam, Orlova A. M. Anna Markovna, Belousov M. V. Mikhail Valerievich, Tolmachev V. M. Vladimir Maksimilianovich, Larkina M. S. Mariya Sergeevna
Shrnutí:Title screen
Noninvasive radionuclide imaging of epithelial cell adhesion molecule (EpCAM) expression in lung, ovarian, breast, kidney, and other cancers can stratify patients for EpCAM-targeted therapy. The constructed scaffold proteins, designed ankyrin repeat proteins (DARPins), are highly specific high-affinity probes for radionuclide imaging. A clinical study demonstrated that the anti-EpCAM DARPin [99mTc]Tc-(HE)3-Ec1 showed precise EpCAM imaging at 2, 4, and 6 h after injection in patients with nonsmall cell lung cancer. However, a noticeable accumulation in healthy organs has prompted the development of new Ec1-based agents with improved biodistribution properties. In addition, it would be desirable to substitute a labor-intensive labeling procedure. The purpose of this study was to test the hypothesis that the use of Gly-Gly-Gly-Cys (G3C) or Glu-Glu-Glu-Cys (E3C) peptide chelators placed at the C-terminus of DARPin for labeling with 99mTc (V) could improve the image contrast and biodistribution of Ec1. The radiochemical yield of the new variants exceeded 95%. The labeled proteins specifically bound to human EpCAM-expressing cancer cell lines with affinities of 8–10 nM. The biodistribution of [99mTc]Tc-Ec1-G3C and [99mTc]Tc-Ec1-E3C in mice was compared with the biodistribution of clinically tested [99mTc]Tc-(HE)3-Ec1 in a Nu/j mouse model with SKOV-3 xenografts. The new variants specifically accumulate in human xenografts with EpCAM expression. The accumulation of new variants in healthy organs (liver, salivary glands, spleen, and stomach) was reduced compared to [99mTc]Tc-(HE)3-Ec1. [99mTc]Tc-Ec1-G3C provided the best imaging contrast and is suitable for clinical testing
AM_Agreement
Jazyk:angličtina
Vydáno: 2026
Témata:
On-line přístup:https://doi.org/10.1021/acs.molpharmaceut.5c01498
Médium: Elektronický zdroj Kapitola
KOHA link:https://koha.lib.tpu.ru/cgi-bin/koha/opac-detail.pl?biblionumber=686119

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200 1 |a The Use of Glycine-Containing Peptide-Based Chelators for Labeling with 99mTc Improves the Imaging Properties of EpCAM-Targeting Designed Ankyrin Repeat Ec1  |f Sergey Deyev, Anastasia Fominykh, Ruslan Varvashenya [et al.] 
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330 |a Noninvasive radionuclide imaging of epithelial cell adhesion molecule (EpCAM) expression in lung, ovarian, breast, kidney, and other cancers can stratify patients for EpCAM-targeted therapy. The constructed scaffold proteins, designed ankyrin repeat proteins (DARPins), are highly specific high-affinity probes for radionuclide imaging. A clinical study demonstrated that the anti-EpCAM DARPin [99mTc]Tc-(HE)3-Ec1 showed precise EpCAM imaging at 2, 4, and 6 h after injection in patients with nonsmall cell lung cancer. However, a noticeable accumulation in healthy organs has prompted the development of new Ec1-based agents with improved biodistribution properties. In addition, it would be desirable to substitute a labor-intensive labeling procedure. The purpose of this study was to test the hypothesis that the use of Gly-Gly-Gly-Cys (G3C) or Glu-Glu-Glu-Cys (E3C) peptide chelators placed at the C-terminus of DARPin for labeling with 99mTc (V) could improve the image contrast and biodistribution of Ec1. The radiochemical yield of the new variants exceeded 95%. The labeled proteins specifically bound to human EpCAM-expressing cancer cell lines with affinities of 8–10 nM. The biodistribution of [99mTc]Tc-Ec1-G3C and [99mTc]Tc-Ec1-E3C in mice was compared with the biodistribution of clinically tested [99mTc]Tc-(HE)3-Ec1 in a Nu/j mouse model with SKOV-3 xenografts. The new variants specifically accumulate in human xenografts with EpCAM expression. The accumulation of new variants in healthy organs (liver, salivary glands, spleen, and stomach) was reduced compared to [99mTc]Tc-(HE)3-Ec1. [99mTc]Tc-Ec1-G3C provided the best imaging contrast and is suitable for clinical testing 
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463 |t Vol. 23, iss. 4  |v P. 2469–2480  |d 2026 
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701 1 |a Fominykh  |b A. S.  |g Anastasiya Sergeevna  |f 1998-  |c chemist  |c Engineer of Tomsk Polytechnic University  |9 88811 
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701 1 |a Bodenko  |b V. V.  |c pharmacist  |c engineer at Tomsk Polytechnic University  |f 1997-  |g Vitalina Vasiljevna  |9 88553 
701 1 |a Plotnikov  |b E. V.  |c chemist  |c Associate Professor of Tomsk Polytechnic University, Candidate of Chemical Sciences  |f 1983-  |g Evgeny Vladimirovich  |9 16417 
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701 1 |a Shulga (Schulga)  |b A. A.  |c biologist  |c Researcher, Tomsk Polytechnic University, Candidate of Biological Sciences  |f 1960-  |g Aleksey Anatolievich  |9 22432 
701 1 |a Konovalova  |b E. V.  |c specialist in the field of chemical technology and biotechnology  |c engineer at Tomsk Polytechnic University  |f 1985-  |g Elena Valerjevna  |9 88562 
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701 1 |a Orlova  |b A. M.  |c specialist in the field of medical technology  |c Senior Researcher, Oncoteranostika Research Center, Tomsk Polytechnic University, Ph.D  |f 1960-  |g Anna Markovna  |9 22212 
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