The position of 99mTc-HYNIC and the molecular design of the DARPin G3 constructs influence the selection of an imaging tracer to detect expression in HER2-expressing tumors; Journal of Radioanalytical and Nuclear Chemistry; Vol. 335

Detalhes bibliográficos
Parent link:Journal of Radioanalytical and Nuclear Chemistry.— .— New York: Springer Science+Business Media LLC.
Vol. 335.— 2026.— P. 1945–1959
Outros Autores: Larkina M. S. Mariya Sergeevna, Varvashenya R. N. Ruslan Nikolaevich, Prach A. A. Anastasiya Aleksandrovna, Plotnikov E. V. Evgeny Vladimirovich, Tretyakova (Tretjyakova) M. S. Maria Sergeevna, Eskova D. D. Darjya Dmitrievna, Bodenko V. V. Vitalina Vasiljevna, Yanovich G. Gleb, Shulga (Schulga) A. A. Aleksey Anatolievich, Konovalova E. V. Elena Valerjevna, Ziganshin R. Rustam, Belousov M. V. Mikhail Valerievich, Chernov V. I. Vladimir Ivanovich, Tolmachev V. M. Vladimir Maksimilianovich, Deev S. M. Sergey Mikhaylovich
Resumo:Title screen
Purpose The objective of the present study was to test the hypothesis that the position of the HYNIC chelator in DARPin G3 variants affects in vivo biodistribution and to select the most effective variant as a 99mTc imaging agent for HER2-expressing tumors. Methods This study evaluated the labelling, affinity, cellular processing, biodistribution, and in vivo targeting specificity of novel N- and C-terminal DARPin G3-HYNIC constructs. In addition, amino acid sequences containing E3C or (G3S)3C at the N- and C-terminus of the protein were used as linkers for HYNIC binding to DARPin G3 to enrich the molecular design of constructs in this study. Results The results demonstrated that the position of the HYNIC chelating group in DARPin G3 constructs did not affect the binding properties of the target in vitro and in vivo. At the same time, the position of HYNIC was found to strongly influence the biodistribution of labelled DARPin G3 constructs in CD1 mice, showing increased accumulation in the kidneys and decreased levels in the liver, spleen, and lungs when HYNIC was added to the N-terminus of the protein variants. Conclusion New N- and C-terminal constructs of DARPin G3-HYNIC were generated for HER2 targeting. It is evident that changing the position of the chelator in DARPin G3-HYNIC leads to differences in pharmacokinetic behaviour. The biodistribution of HYNIC variants attached to the N- or C-terminus of DARPin G3 was not significantly altered by different amino acid linkers. Therefore, variants with HYNIC positioned at the N-terminus are more useful for selecting a 99mTc-DARPin G3 imaging tracer. The [99mTc]Tc-HYNIC-C(G3S)3-G3 variant exhibited enhanced biodistribution compared to [99mTc]Tc-HYNIC-CE3-G3, particularly regarding reduced uptake in the liver
AM_Agreement
Idioma:inglês
Publicado em: 2026
Assuntos:
Acesso em linha:https://doi.org/10.1007/s10967-026-10739-w
Formato: Recurso Eletrônico Capítulo de Livro
KOHA link:https://koha.lib.tpu.ru/cgi-bin/koha/opac-detail.pl?biblionumber=686120

MARC

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200 1 |a The position of 99mTc-HYNIC and the molecular design of the DARPin G3 constructs influence the selection of an imaging tracer to detect expression in HER2-expressing tumors  |f Maria Larkina, Ruslan Varvashenya, Anastasia Prach [et al.] 
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330 |a Purpose The objective of the present study was to test the hypothesis that the position of the HYNIC chelator in DARPin G3 variants affects in vivo biodistribution and to select the most effective variant as a 99mTc imaging agent for HER2-expressing tumors. Methods This study evaluated the labelling, affinity, cellular processing, biodistribution, and in vivo targeting specificity of novel N- and C-terminal DARPin G3-HYNIC constructs. In addition, amino acid sequences containing E3C or (G3S)3C at the N- and C-terminus of the protein were used as linkers for HYNIC binding to DARPin G3 to enrich the molecular design of constructs in this study. Results The results demonstrated that the position of the HYNIC chelating group in DARPin G3 constructs did not affect the binding properties of the target in vitro and in vivo. At the same time, the position of HYNIC was found to strongly influence the biodistribution of labelled DARPin G3 constructs in CD1 mice, showing increased accumulation in the kidneys and decreased levels in the liver, spleen, and lungs when HYNIC was added to the N-terminus of the protein variants. Conclusion New N- and C-terminal constructs of DARPin G3-HYNIC were generated for HER2 targeting. It is evident that changing the position of the chelator in DARPin G3-HYNIC leads to differences in pharmacokinetic behaviour. The biodistribution of HYNIC variants attached to the N- or C-terminus of DARPin G3 was not significantly altered by different amino acid linkers. Therefore, variants with HYNIC positioned at the N-terminus are more useful for selecting a 99mTc-DARPin G3 imaging tracer. The [99mTc]Tc-HYNIC-C(G3S)3-G3 variant exhibited enhanced biodistribution compared to [99mTc]Tc-HYNIC-CE3-G3, particularly regarding reduced uptake in the liver  
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461 1 |t Journal of Radioanalytical and Nuclear Chemistry  |c New York  |n Springer Science+Business Media LLC. 
463 |t Vol. 335  |v P. 1945–1959  |d 2026 
610 1 |a труды учёных ТПУ 
610 1 |a электронный ресурс 
610 1 |a Designed ankyrin repeat proteins 
610 1 |a HER2 
610 1 |a Imaging 
610 1 |a HYNIC 
610 1 |a 99mTc 
701 1 |a Larkina  |b M. S.  |g Mariya Sergeevna  |f 1984-  |c pharmacist  |c Professor; Senior Researcher of the Tomsk Polytechnic University, Doctor of Pharmaceutical Sciences  |9 22417 
701 1 |a Varvashenya  |b R. N.  |c pharmacist  |c engineer at Tomsk Polytechnic University  |f 1997-  |g Ruslan Nikolaevich  |9 88559 
701 1 |a Prach  |b A. A.  |g Anastasiya Aleksandrovna  |f 1999-  |c chemist  |c engineer of Tomsk Polytechnic University  |9 88930 
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 
701 1 |a Tretyakova (Tretjyakova)  |b M. S.  |c Medical technology specialist  |c Research Engineer of Tomsk Polytechnic University  |f 1994-  |g Maria Sergeevna  |9 22127 
701 1 |a Eskova  |b D. D.  |g Darjya Dmitrievna  |f 2003-  |c biotechnologist  |c laboratory assistant of Tomsk Polytechnic University  |9 88808 
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 Yanovich  |b G.  |c Pharmacist  |c engineer of Tomsk Polytechnic University  |f 1999-  |g Gleb  |9 89205 
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 
701 1 |a Ziganshin  |b R.  |g Rustam 
701 1 |a Belousov  |b M. V.  |c chemist  |c Professor of Tomsk Polytechnic University, Doctor of Pharmaceutical Sciences  |f 1963-  |g Mikhail Valerievich  |9 21924 
701 1 |a Chernov  |b V. I.  |c specialist in the field of medical technology  |c lead engineer of Tomsk Polytechnic University, doctor of medical sciences  |f 1962-  |g Vladimir Ivanovich  |9 17725 
701 1 |a Tolmachev  |b V. M.  |c specialist in the field of medical technology  |c Director of the Research Center "Oncoteranostika", Tomsk Polytechnic University, Ph.D  |f 1961-  |g Vladimir Maksimilianovich  |9 22210 
701 1 |a Deev  |b S. M.  |c biologist  |c Leading Researcher, Tomsk Polytechnic University, Doctor of Biological Sciences  |f 1951-  |g Sergey Mikhaylovich  |9 20959 
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