Investigating the time resolution of a compact multidimensional gamma-spectrometer

Burnett, Jonathan L.; Davies, A. V.

doi:10.1007/s10967-011-1017-y

Cited by 23 publications

(5 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…SPECT is a powerful technique for taking low-level nuclear measurements (28). In the present study, the imaging value of 131 I-K237 in LNCaP xenografts was investigated.…”

Section: Discussionmentioning

confidence: 96%

A novel molecular probe 131I-K237 targeting tumor angiogenesis in human prostate cancer xenografts

Zhao

Guo

2012

Molecular Medicine Reports

View full text Add to dashboard Cite

Specific molecular probes are essential for the early diagnosis of prostate cancer. In addition, peptides have been shown to have numerous uses as diagnostic and therapeutic molecular probes. The K237 peptide binds to the vascular endothelial growth factor receptor with high affinity and specificity, and was predicted to have potential use as a probe in tumor angiogenesis. The overall aim of the present study was to assess the diagnostic potential of 131I‑K237 as a molecular probe for prostate cancer. The K237 peptide was radiolabeled with 131I using an Iodogen method. The radiolabeling efficiency and radiochemical purity were found to be 73.7 ± 3.2 and 96.7 ± 0.6%, respectively, which were determined using thin layer chromatography and high performance liquid chromatography in vitro. Cellular uptake and competition binding experiments were used to identify the affinity of 131I‑K237 to LNCaP prostate cancer cells. The binding ratio of 131I‑K237 to LNCaP cells in the experimental group was 95.8 ± 1.5%, whereas the binding ratios in the 5 kBq Na131I, 10 kBq Na131I, 15 kBq Na131I and PBS groups were 8.2 ± 0.4, 8.3 ± 0.2, 8.5 ± 0.2 and 0.0%, respectively. In addition, the binding ratio of 131I‑K237 to LNCaP significantly decreased with the increased dose of unlabeled K237. A total of 40 male BALB/c mice with LNCaP xenografts were used for biodistribution and single photon emission computed tomography imaging analysis. An image was obtained and tumors were visible from 2 h post injection of 131I‑K237. In conclusion, the results of the present study showed that 131I‑K237 had a high affinity for LNCaP cells and may be considered as a candidate diagnostic molecular probe for prostate cancer.

show abstract

“…SPECT is a powerful technique for taking low-level nuclear measurements (28). In the present study, the imaging value of 131 I-K237 in LNCaP xenografts was investigated.…”

Section: Discussionmentioning

confidence: 96%

A novel molecular probe 131I-K237 targeting tumor angiogenesis in human prostate cancer xenografts

Zhao

Guo

2012

Molecular Medicine Reports

View full text Add to dashboard Cite

show abstract

“…[ 47 ]; (v) beta-gamma-gamma coincidence mode (e.g. [ 47 ]; (vi) multidimensional gamma-spectrometer [ 47 , 52 , 53 ]; (vii) gamma–gamma spectrometer for measuring angular distribution of gamma-quanta. Coincidence gamma-spectrometers may decrease a background by about two orders of magnitude, what makes these spectrometers superior for very low-level gamma-spectrometry of positron or cascade gamma-emitters (e.g.…”

Section: Development Of Radiometric Technologiesmentioning

confidence: 99%

“…The recent developments in low-level radioanalytical techniques have helped to improve the detection limits using: (i) High efficiency Ge detectors (up to 200% of relative efficiency compared to 76 mm in diameter and 76 mm long NaI(Tl) crystal) operating in underground laboratories which represent the most important achievement in radiometric analysis of radionuclides [ 1 – 4 , 18 – 26 , 35 , 36 ]; (ii) Anticosmic shielding of detectors operating in surface and shallow-depth underground laboratories [ 39 – 42 ] which helped to improve detection limits comparable to deeper underground laboratories; (iii) Multidetector coincidence gamma-spectrometry systems for analysis of cascade and/or positron emitters [ 43 – 51 ]; (iv) Multidimensional gamma-spectrometry [ 52 , 53 ]. Thanks to excellent energy resolution of Ge detectors (< 2 keV for 1.33 MeV gamma-rays), and possibility to analyse various gamma-emitters in material and environmental samples selectively and very often non-destructively, they dominated in the field of ultra-low-level gamma-spectrometry [ 54 – 60 ].…”

Section: Introductionmentioning

confidence: 99%

New ultra-sensitive radioanalytical technologies for new science

Povinec

2018

J Radioanal Nucl Chem

View full text Add to dashboard Cite

Recent developments in radiometric and mass spectrometry technologies have been associated in the radiometric sector mainly with underground operations of large volume Ge detectors, while the mass-spectrometry sector, represented mainly by accelerator mass spectrometry and inductively coupled plasma mass spectrometry has become the most sensitive technique for ultra-low-level analyses of long-lived radionuclides. These new developments have had great impact on investigations of rare nuclear processes and applications of radionuclides in environmental, life and space sciences. New scientific investigations have been carried out therefore which have not been possible before either because of lack of sensitivity or required large sample size.

show abstract

“…The present micro-SPECT/CT imaging study of 125 I−F56 and coadministration of F56 peptide block agent in mice xenografted with BGC-823 tumor demonstrated that the technique can give both functional and anatomic information from organism, if it is used with high binding radiotracer at nanomolar range. 16 Recent studies revealed that overexpression of VEGFR1 may cause poor disease outcome in various cancer types, including GCa. 17−20 Furthermore, there is also a consistent association between high VEGFR1 level and the relapse of surgically treated patients.…”

Section: Acs Medicinal Chemistry Lettersmentioning

confidence: 99%

¹²⁵I–F56 Peptide as Radioanalysis Agent Targeting VEGFR1 in Mice Xenografted with Human Gastric Tumor

Zhu

Zhao

Liu

et al. 2017

ACS Med. Chem. Lett.

View full text Add to dashboard Cite

I-Radiolabeled F56 peptide was designed as a radioactive analogue of F56 (peptide WHSDMEWWYLLG) to bind with VEGFR1 receptor. It was synthesized in high radiochemical yield and specific activity. The stability ofI-F56 was tested, and the bioactivity of I-F56 was confirmed by both cell uptake and binding affinity measurement in VEGFR1 positive BGC-823 cells. The time-radioactivity relationship and biodistribution ofI-F56 tracer were conducted using nude mice bearing human gastric carcinoma BGC-823, by noninvasive micro-SPECT/CT imaging. The tracer's tumor uptake was further confirmed by autoradiography and HE stain of I-F56 in tumor tissues ex vivo. Those results demonstrated thatI-F56 holds great potential as a diagnostic agent in both molecular imaging and radioanalysis probe for gastric cancer.

show abstract

Investigating the time resolution of a compact multidimensional gamma-spectrometer

Cited by 23 publications

References 4 publications

A novel molecular probe 131I-K237 targeting tumor angiogenesis in human prostate cancer xenografts

A novel molecular probe 131I-K237 targeting tumor angiogenesis in human prostate cancer xenografts

New ultra-sensitive radioanalytical technologies for new science

¹²⁵I–F56 Peptide as Radioanalysis Agent Targeting VEGFR1 in Mice Xenografted with Human Gastric Tumor

Contact Info

Product

Resources

About

Investigating the time resolution of a compact multidimensional gamma-spectrometer

Cited by 23 publications

References 4 publications

A novel molecular probe 131I-K237 targeting tumor angiogenesis in human prostate cancer xenografts

A novel molecular probe 131I-K237 targeting tumor angiogenesis in human prostate cancer xenografts

New ultra-sensitive radioanalytical technologies for new science

125I–F56 Peptide as Radioanalysis Agent Targeting VEGFR1 in Mice Xenografted with Human Gastric Tumor

Contact Info

Product

Resources

About

¹²⁵I–F56 Peptide as Radioanalysis Agent Targeting VEGFR1 in Mice Xenografted with Human Gastric Tumor