Comparative Evaluation of Two DARPin Variants: Effect of Affinity, Size, and Label on Tumor Targeting Properties; ACS Molecular Pharmaceutics; Vol. 16, No. 3

Detalles Bibliográficos
Parent link:ACS Molecular Pharmaceutics
Vol. 16, No. 3.— 2019.— [P. 995–1008]
Autor Corporativo: Национальный исследовательский Томский политехнический университет Физико-технический институт Лаборатория № 31 ядерного реактора
Otros Autores: Deev S. M. Sergey Mikhaylovich, Vorobjeva (Vorobyeva) A. G. Anzhelika Grigorjevna, Shulga (Schulga) A. A. Aleksey Anatolievich, Proshkina G. M. Galina Mikhaylovna, Guler R. Rezan, Lofblom J. John, Mitran B. Bogdan, Garousi J. Javad, Altai M. Mohamed, Buijs J. Jos, Chernov V. I. Vladimir Ivanovich, Orlova A. M. Anna Markovna, Tolmachev V. M. Vladimir Maksimilianovich
Sumario:Title screen
Designed ankyrin repeat proteins (DARPins) are small engineered scaffold proteins that can be selected for binding to desirable molecular targets. High affinity and small size of DARPins render them promising probes for radionuclide molecular imaging. However, detailed knowledge on many factors influencing their imaging properties is still lacking. We have evaluated two human epidermal growth factor 2 (HER2)-specific DARPins with different size and binding properties. DARPins 9_29-H6 and G3-H6 were radiolabeled with iodine-125 and tricarbonyl technetium-99m and evaluated in vitro. A side-by-side comparison of biodistribution and tumor targeting was performed. HER2-specific tumor accumulation of G3-H6 was demonstrated. A combination of smaller size and higher affinity resulted in a higher tumor uptake of G3-H6 in comparison to 9_29-H6. Technetium-99m labeled G3-H6 demonstrated a better biodistribution profile than 9_29-H6, with several-fold lower uptake in liver. Radioiodinated G3-H6 showed the best tumor-to-organ ratios. The combined effect of affinity, molecular weight, scaffold composition, and nonresidualizing properties of iodine label provided radioiodinated G3-H6 with high clinical potential for imaging of HER2.
Режим доступа: по договору с организацией-держателем ресурса
Lenguaje:inglés
Publicado: 2019
Materias:
Acceso en línea:https://doi.org/10.1021/acs.molpharmaceut.8b00922
Formato: Electrónico Capítulo de libro
KOHA link:https://koha.lib.tpu.ru/cgi-bin/koha/opac-detail.pl?biblionumber=664012

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200 1 |a Comparative Evaluation of Two DARPin Variants: Effect of Affinity, Size, and Label on Tumor Targeting Properties  |f S. M. Deev, A. Vorobjeva, A. A. Schulga [et al.] 
203 |a Text  |c electronic 
300 |a Title screen 
330 |a Designed ankyrin repeat proteins (DARPins) are small engineered scaffold proteins that can be selected for binding to desirable molecular targets. High affinity and small size of DARPins render them promising probes for radionuclide molecular imaging. However, detailed knowledge on many factors influencing their imaging properties is still lacking. We have evaluated two human epidermal growth factor 2 (HER2)-specific DARPins with different size and binding properties. DARPins 9_29-H6 and G3-H6 were radiolabeled with iodine-125 and tricarbonyl technetium-99m and evaluated in vitro. A side-by-side comparison of biodistribution and tumor targeting was performed. HER2-specific tumor accumulation of G3-H6 was demonstrated. A combination of smaller size and higher affinity resulted in a higher tumor uptake of G3-H6 in comparison to 9_29-H6. Technetium-99m labeled G3-H6 demonstrated a better biodistribution profile than 9_29-H6, with several-fold lower uptake in liver. Radioiodinated G3-H6 showed the best tumor-to-organ ratios. The combined effect of affinity, molecular weight, scaffold composition, and nonresidualizing properties of iodine label provided radioiodinated G3-H6 with high clinical potential for imaging of HER2. 
333 |a Режим доступа: по договору с организацией-держателем ресурса 
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461 |t ACS Molecular Pharmaceutics 
463 |t Vol. 16, No. 3  |v [P. 995–1008]  |d 2019 
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610 1 |a I-125 
610 1 |a Tc-99m 
610 1 |a радионуклиды 
610 1 |a визуализация 
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701 1 |a Deev  |b S. M.  |c biologist  |c Leading Researcher, Tomsk Polytechnic University, Doctor of Biological Sciences  |f 1951-  |g Sergey Mikhaylovich  |3 (RuTPU)RU\TPU\pers\39299  |9 20959 
701 1 |a Vorobjeva (Vorobyeva)  |b A. G.  |c specialist in the field of medical technology  |c Senior Researcher, Oncoteranostika Research Center, Tomsk Polytechnic University, Ph.D  |f 1990-  |g Anzhelika Grigorjevna  |9 22214 
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 Proshkina  |b G. M.  |g Galina Mikhaylovna 
701 1 |a Guler  |b R.  |g Rezan 
701 1 |a Lofblom  |b J.  |g John 
701 1 |a Mitran  |b B.  |g Bogdan 
701 1 |a Garousi  |b J.  |g Javad 
701 1 |a Altai  |b M.  |g Mohamed 
701 1 |a Buijs  |b J.  |g Jos 
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  |3 (RuTPU)RU\TPU\pers\34191  |9 17725 
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 
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 
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