New chelation strategy allows for quick and clean 99mTc-labeling of synthetic peptides

Blok, D.; Feitsma, H. I. J.; Kooy, Yvonne; Welling, Mick M.; Ossendorp, Ferry; Vermeij, P.; Drijfhout, Jan W.

doi:10.1016/j.nucmedbio.2004.02.009

Cited by 17 publications

(7 citation statements)

References 18 publications

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“…Bifunctional chelating agents such as MAG3, N2S2, tripeptide triamino-thiol (N3S), S4, P2S2, DTPA, 2-picolylamine- N,N -diacetate and the Nα-histidinyl acetatecarbonyl have been used for stabilization of the radioactive metal center under in vivo conditions. Other chelators have also been proposed to conjugate 99m Tc to active biological components, such as PNP and HYNIC [35]. In this context, many studies utilizing 99m Tc labeled-bombesin have been described and a summary can be found in Table 4.…”

Section: Radiolabeled Bbn Derivatives In Preclinical Studiesmentioning

confidence: 99%

Radiolabeled bombesin derivatives for preclinical oncological imaging

Ferreira

Fuscaldi

Townsend

et al. 2017

Biomedicine & Pharmacotherapy

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Despite efforts, cancer is still one of the leading causes of morbidity and mortality worldwide, with approximately 14 million new cases and 8.2 million cancer-related deaths each year, according to the World Health Organization. Among the strategies to reduce cancer progression and improving its management, implementing early detection technologies is crucial. Based on the fact that several types of cancer cells overexpress surface receptors, small molecule ligands, such as peptides, have been developed to allow tumor identification at earlier stages. Allied with imaging techniques such as PET and SPECT, radiolabeled peptides play a pivotal role in nuclear medicine. Bombesin, a peptide of 14 amino acids, is an amphibian homolog to the mammalian gastrin-releasing peptide (GRP), that has been extensively studied as a targeting ligand for diagnosis and therapy of GRP positive tumors, such as breast, pancreas, lungs and prostate cancers. In this context, herein we provide a review of reported bombesin derivatives radiolabeled with a multitude of radioactive isotopes for diagnostic purposes in the preclinical setting. Moreover, since animal models are highly relevant for assessing the potential of clinical translation of this radiopeptides, a brief report of the currently used GRP-positive tumor-bearing animal models is described.

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Section: Radiolabeled Bbn Derivatives In Preclinical Studiesmentioning

confidence: 99%

Radiolabeled bombesin derivatives for preclinical oncological imaging

Ferreira

Fuscaldi

Townsend

et al. 2017

Biomedicine & Pharmacotherapy

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“…This analogue showed good GRP-R-targeting in mice and excretion via the renal pathway [28,29] . Neutral 99m Tc V O 3+ -complexes are also obtained by coupling tripeptide N 3 S-donors to BB or BB (7)(8)(9)(10)(11)(12)(13)(14), either directly or via a spacer [30][31][32][33][34] . For example, 99m Tc-RP527, a BB (7)(8)(9)(10)(11)(12)(13)(14) analogue linked at the N-terminus via a glycine-5-aminovaleric acid spacer to the tri-peptide chelator, dimethylglycyl-L-ser-L-cys, reached a 2%ID/g at 1 h pi in PC-3 xenografts in SCID (severe combined immunodeficiency) mice [30,31] .…”

Section: Development and Preclinical Studies On Radiolabelled Bombesinsmentioning

confidence: 99%

Targeting prostate cancer with radiolabelled bombesins

Maina

Nock²,

Mather

2006

Cancer Imaging

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The fact that a number of common human tumours, including those of breast and prostate, express increased levels of the gastrin-releasing peptide receptor (GRP-R) means that this receptor is a potential target for peptide receptor mediated scintigraphy and targeted radionuclide therapy. Although clinical application is yet in its infancy, there is a considerable literature on preclinical studies aimed at developing suitable radioligands for potential clinical application. This brief review provides an overview of this research and also describes some of the limited clinical studies that have been published.

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“…Therefore, accessible hCyp18 cysteine residues might rather act as intermediary stabilizing agents that prevent fast reoxidation of Re (+V) salts in water as reported for gluconate and tartrate. 28,29 Although we used high concentrations (64 mM) in protein, the lack of detectable adducts might be explained by the relatively low yields of complexes that implies that cyclophilin oxidation is rather marginal relative to the effective concentration in components and protein. The exact role of Cys52 and Cys62 would also have to be delineated.…”

Section: Discussionmentioning

confidence: 99%

Implication of cysteine residues in the selection of oxorhenium inhibitors of cyclophilin hCyp18

et al. 2012

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The dynamic combinatorial assembly of libraries of modular cyclophilin hCyp18 oxorhenium inhibitors of general formula [A˙ReO˙B] was accelerated by addition of increasing concentrations of hCyp18 ('Cyclophilin Enhancing Effect', CEE). This result suggested that modules assembly might proceed through an in situ coordination chemistry process. However, we observed that the CEE was not strictly related to the affinity of the complexes for hCyp18. The CEE was not altered by cyclosporine A, a potent competitive inhibitor of hCyp18. The use of a non-degassed buffer caused a fall in complexation yields that could be reversed upon addition of hCyp18. All these data suggested that the CEE results from a partial protection of exogenous thiols against reoxidation. As anticipated, carbamido-methylation of cyclophilin Cys52 and Cys62 residues with iodoacetamide annihilated the CEE. All these results highlight the role of hCyp18 in maintaining chemical modules in a reduced state.

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New chelation strategy allows for quick and clean 99mTc-labeling of synthetic peptides

Cited by 17 publications

References 18 publications

Radiolabeled bombesin derivatives for preclinical oncological imaging

Radiolabeled bombesin derivatives for preclinical oncological imaging

Targeting prostate cancer with radiolabelled bombesins

Implication of cysteine residues in the selection of oxorhenium inhibitors of cyclophilin hCyp18

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