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An improved method of 18F peptide labeling: hydrazone formation with HYNIC-conjugated c(RGDyK)

Authors
 Yun-Sang Lee  ;  Jae Min Jeong  ;  Hyung Woo Kim  ;  Young Soo Chang  ;  Young Joo Kim  ;  Mee Kyung Hong  ;  Ganesha B. Rai  ;  Dae Yoon Chi  ;  Won Jun Kang  ;  Joo Hyun Kang  ;  Dong Soo Lee  ;  June-Key Chung  ;  Myung Chul Lee  ;  Young-Ger Suh 
Citation
 NUCLEAR MEDICINE AND BIOLOGY, Vol.33(5) : 677-683, 2006 
Journal Title
NUCLEAR MEDICINE AND BIOLOGY
ISSN
 0969-8051 
Issue Date
2006
MeSH
Animals ; Fluorine Radioisotopes/chemistry ; Fluorine Radioisotopes/pharmacokinetics ; Hydrazines/chemistry ; Hydrazines/pharmacokinetics ; Hydrazones/chemistry ; Hydrazones/pharmacokinetics ; Integrin alphaVbeta3/chemistry ; Integrin alphaVbeta3/metabolism* ; Ischemia/diagnostic imaging* ; Ischemia/metabolism* ; Isotope Labeling/methods ; Metabolic Clearance Rate ; Mice ; Muscle, Skeletal/blood supply ; Muscle, Skeletal/diagnostic imaging* ; Muscle, Skeletal/metabolism* ; Nicotinic Acids/chemistry ; Nicotinic Acids/pharmacokinetics ; Oligopeptides/chemistry ; Oligopeptides/pharmacokinetics* ; Organ Specificity ; Radionuclide Imaging ; Radiopharmaceuticals/chemical synthesis ; Radiopharmaceuticals/pharmacokinetics ; Tissue Distribution
Keywords
Peptide labeling ; 18F ; αvβ3-Integrin ; RGD peptide ; HYNIC ; [18F]Fluorobenzaldehyde
Abstract
Radiolabeled αvβ3-integrin antagonists are increasingly investigated as a means of imaging angiogenesis. Several methods of labeling αvβ3-integrin binding peptide with 18F have been reported recently. In the present study, we devised a straightforward means for labeling Arg–Gly–Asp (RGD) peptide with 18F via hydrazone formation between c(RGDyK)-hydrazinonicotinic acid (HYNIC) (3) and 4-[18F]-fluorobenzaldehyde ([18F]4). The resulting reaction mixture was purified by HPLC to give 4′-[18F]-fluorobenzylidenehydrazone-6-nicotinamide-c(RGDyK) ([18F]5). The conjugation efficiency of 3 and 4 to form [18F]5 was 95.2%, and the radiochemical purity of [18F]5 after purification was >99%. The specific activity of [18F]5 estimated by radio-HPLC was 20.5 GBq/μmol (end of synthesis). Competitive binding assay of c(RGDyK) (1) and 5 was performed using [125I]iodo-c(RGDyK) as a radioligand, and Ki values were found to be 2.8 and 21.7 nM, respectively. For the biodistribution study, the angiogenic mouse model was established by inducing unilateral ischemia on the left hindlimbs of ICR mice after femoral artery ablation. Seven days after inducing ischemia, [18F]5 was administered to the mice through the tail vein. Ischemic muscle uptake of [18F]5 was significantly higher than that of normal muscle (P<.01). Specific uptake was confirmed by coinjection of 1 with [18F]5. Here, we successfully labeled RGD peptide with 18F via hydrazone formation between 3 and 4, resulting to [18F]5. [18F]5 was found to have high affinity for αvβ3-integrin and to accumulate specifically in ischemic hindlimb muscle of mice. We suggest that 18F labeling via formation of hydrazone between HYNIC peptide and [18F]4 is a useful method for labeling c(RGDyK), which can be applied for imaging angiogenesis.
Full Text
http://www.sciencedirect.com/science/article/pii/S0969805106000709
DOI
10.1016/j.nucmedbio.2006.04.004
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Nuclear Medicine (핵의학교실) > 1. Journal Papers
Yonsei Authors
Kang, Won Jun(강원준) ORCID logo https://orcid.org/0000-0002-2107-8160
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/111006
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