EGF receptor targeted tumor imaging with biotin-PEG-EGF linked to Tc-99m-HYNIC labeled avidin and streptavidin
- Authors
- Jung, KH[Jung, Kyung-Ho]; Park, JW[Park, Jin Won]; Paik, JY[Paik, Jin-Young]; Cung, HTQ[Cung Hoa Thien Quach]; Choe, YS[Choe, Yearn Seong]; Lee, KH[Lee, Kyung-Han]
- Issue Date
- Nov-2012
- Publisher
- ELSEVIER SCIENCE INC
- Keywords
- Epidermal growth factor; Receptor imaging; Strepta
- Citation
- NUCLEAR MEDICINE AND BIOLOGY, v.39, no.8, pp.1122 - 1127
- Indexed
- SCIE
SCOPUS
- Journal Title
- NUCLEAR MEDICINE AND BIOLOGY
- Volume
- 39
- Number
- 8
- Start Page
- 1122
- End Page
- 1127
- URI
- https://scholarworks.bwise.kr/skku/handle/2021.sw.skku/63701
- DOI
- 10.1016/j.nucmedbio.2012.06.007
- ISSN
- 0969-8051
- Abstract
- Introduction: As direct radiolabeled peptides suffer limitations for in vivo imaging, we investigated the usefulness of radioloabeled avidin and streptavidin as cores to link peptide ligands for targeted tumor imaging. Methods: Human epidermal growth factor (EGF) was site specifically conjugated with a single PEG-biotin molecule and linked to Tc-99m-HYNIC labeled avidin-FITC (Av) or streptavidin-Cy5.5 (Say). Receptor targeting was verified in vitro, and in vivo pharmacokinetic and biodistribution profiles were studied in normal mice. Scintigraphic imaging was performed in MDA-MB-468 breast tumor xenografted nude mice. Results: Whereas both Tc-99m-Av-EGF and Tc-99m-Sav-EGF retained receptor-specific binding in vitro, the two probes substantially diverged in pharmacokinetic and biodistribution behavior in vivo. 99mTc-Av-EGF was rapidly eliminated from the circulation with a T1/2 of 4.3 min, and showed intense hepatic accumulation but poor tumor uptake (0.6%ID/gm at 4 h). Tc-99m-Sav-EGF displayed favorable in vivo profiles of longer circulation (T1/2 beta, 51.5 min) and lower nonspecific uptake that resulted in higher tumor uptake (3.8 %ID/gm) and clear tumor visualization at 15 h. Conclusion: Tc-99m-HYNIC labeled streptavidin linked with growth factor peptides may be useful as a protein-ligand complex for targeted imaging of tumor receptors. (C) 2012 Elsevier Inc. All rights reserved.
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Collections - Medicine > Department of Medicine > 1. Journal Articles
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