Compounds > 2-(4-isothiocyanatobenzyl)-1-4-7-triazacyclononane-1-4-7-triacetic-acid

2-(4-isothiocyanatobenzyl)-1-4-7-triazacyclononane-1-4-7-triacetic-acid and Cell-Transformation--Neoplastic

2-(4-isothiocyanatobenzyl)-1-4-7-triazacyclononane-1-4-7-triacetic-acid has been researched along with Cell-Transformation--Neoplastic* in 1 studies

Other Studies

1 other study(ies) available for 2-(4-isothiocyanatobenzyl)-1-4-7-triazacyclononane-1-4-7-triacetic-acid and Cell-Transformation--Neoplastic

Article	Year
In vitro and in vivo evaluation of a 64Cu-labeled NOTA-Bn-SCN-Aoc-bombesin analogue in gastrin-releasing peptide receptor expressing prostate cancer. Nuclear medicine and biology, 2012, Volume: 39, Issue:5 Bombesin (BN) is an amphibian peptide that binds to the gastrin-releasing peptide receptor (GRPR). It has been demonstrated that BN analogues can be radiolabeled for potential diagnosis and treatment of GRPR-expressing malignancies. Previous studies have conjugated various chelators to the eight C-terminal amino acids of BN [BN(7-14)] for radiolabeling with 64Cu. Recently, (1,4,7-triazacyclononane-1,4,7-triacetic acid) (NOTA) has been evaluated as the five-coordinate 64Cu complex, with results indicating GRPR-specific tumor uptake. This study aimed to conjugate S-2-(4-isothiocyanatobenzyl)-NOTA (p-SCN-Bn-NOTA) to BN(7-14) such that it could form a six-coordinate complex with 64Cu and to evaluate the resulting peptide.. p-SCN-NOTA was conjugated to 8-aminooctanoic acid (Aoc)-BN(7-14) in solution to yield NOTA-Bn-SCN-Aoc-BN(7-14). The unlabeled peptide was evaluated in a cell binding assay using PC-3 prostate cancer cells and 125I-Tyr4-BN to determine the IC50 value. The peptide was radiolabeled with 64Cu and evaluated for internalization into PC-3 cells and for tumor uptake in mice bearing PC-3 xenografts using biodistribution and micro-positron emission tomography imaging studies.. The binding assay demonstrated that NOTA-Bn-SCN-Aoc-BN(7-14) bound with high affinity to GRPR with an IC50 of 1.4 nM. The radiolabeled peptide demonstrated time-dependent internalization into PC-3 cells. In vivo, the peptide demonstrated tumor-specific uptake and imaging that were comparable to those of previously reported 64Cu-labeled BN analogues.. These studies demonstrate that 64Cu-NOTA-Bn-SCN-Aoc-BN(7-14) binds to GRPR-expressing cells and that it can be used for imaging of GRPR-expressing prostate cancer. Topics: Animals; Binding, Competitive; Biological Transport; Bombesin; Caprylates; Cell Line, Tumor; Cell Transformation, Neoplastic; Copper Radioisotopes; Female; Gene Expression Regulation, Neoplastic; Heterocyclic Compounds; Humans; Isothiocyanates; Isotope Labeling; Male; Mice; Multimodal Imaging; Positron-Emission Tomography; Prostatic Neoplasms; Receptors, Bombesin; Tomography, X-Ray Computed	2012

Article

Year

In vitro and in vivo evaluation of a 64Cu-labeled NOTA-Bn-SCN-Aoc-bombesin analogue in gastrin-releasing peptide receptor expressing prostate cancer.

Nuclear medicine and biology, 2012, Volume: 39, Issue:5

Bombesin (BN) is an amphibian peptide that binds to the gastrin-releasing peptide receptor (GRPR). It has been demonstrated that BN analogues can be radiolabeled for potential diagnosis and treatment of GRPR-expressing malignancies. Previous studies have conjugated various chelators to the eight C-terminal amino acids of BN [BN(7-14)] for radiolabeling with 64Cu. Recently, (1,4,7-triazacyclononane-1,4,7-triacetic acid) (NOTA) has been evaluated as the five-coordinate 64Cu complex, with results indicating GRPR-specific tumor uptake. This study aimed to conjugate S-2-(4-isothiocyanatobenzyl)-NOTA (p-SCN-Bn-NOTA) to BN(7-14) such that it could form a six-coordinate complex with 64Cu and to evaluate the resulting peptide.. p-SCN-NOTA was conjugated to 8-aminooctanoic acid (Aoc)-BN(7-14) in solution to yield NOTA-Bn-SCN-Aoc-BN(7-14). The unlabeled peptide was evaluated in a cell binding assay using PC-3 prostate cancer cells and 125I-Tyr4-BN to determine the IC50 value. The peptide was radiolabeled with 64Cu and evaluated for internalization into PC-3 cells and for tumor uptake in mice bearing PC-3 xenografts using biodistribution and micro-positron emission tomography imaging studies.. The binding assay demonstrated that NOTA-Bn-SCN-Aoc-BN(7-14) bound with high affinity to GRPR with an IC50 of 1.4 nM. The radiolabeled peptide demonstrated time-dependent internalization into PC-3 cells. In vivo, the peptide demonstrated tumor-specific uptake and imaging that were comparable to those of previously reported 64Cu-labeled BN analogues.. These studies demonstrate that 64Cu-NOTA-Bn-SCN-Aoc-BN(7-14) binds to GRPR-expressing cells and that it can be used for imaging of GRPR-expressing prostate cancer.

Topics: Animals; Binding, Competitive; Biological Transport; Bombesin; Caprylates; Cell Line, Tumor; Cell Transformation, Neoplastic; Copper Radioisotopes; Female; Gene Expression Regulation, Neoplastic; Heterocyclic Compounds; Humans; Isothiocyanates; Isotope Labeling; Male; Mice; Multimodal Imaging; Positron-Emission Tomography; Prostatic Neoplasms; Receptors, Bombesin; Tomography, X-Ray Computed

2012