In vivo evaluation of 99mTc/188Re-labeled linear alpha-melanocyte stimulating hormone analogs for specific melanoma targeting.

  title={In vivo evaluation of 99mTc/188Re-labeled linear alpha-melanocyte stimulating hormone analogs for specific melanoma targeting.},
  author={J Chen and Michael F. Giblin and N. Wang and Silvia S. Jurisson and Thomas P. Quinn},
  journal={Nuclear medicine and biology},
  volume={26 6},
Melanoma-targeting properties of (99m)technetium-labeled cyclic alpha-melanocyte-stimulating hormone peptide analogues.
The compact cyclic structure of 99mTc-CCMSH, its resistance to degradation, and its enhanced intracellular retention are the major contributing factors to the superior in vivo tumor targeting properties of 99tc- CCMSH.
Melanoma targeting with [99mTc(N)(PNP3)]-labeled α-melanocyte stimulating hormone peptide analogs: Effects of cyclization on the radiopharmaceutical properties.
Design and evaluation of new Tc-99m-labeled lactam bridge-cyclized alpha-MSH peptides for melanoma imaging.
Overall, high melanoma uptake coupled with fast urinary clearance of (99m)Tc(EDDA)-HYNIC-GGNle-CycMSH(hex) highlighted its potential for metastatic melanoma detection in the future.
Radiochemical and radiopharmacological characterization of a 64 Cu-labeled α-MSH analog conjugated with different chelators.
The three 64 Cu-labeled conjugates exhibited high binding affinity (low nanomolar range) in murine B16F10, human MeWo, and human TXM13 cells, and should be considered for further in vivo investigations using a suitable xenograft mouse model.
Evaluation of an (111)In-DOTA-rhenium cyclized alpha-MSH analog: a novel cyclic-peptide analog with improved tumor-targeting properties.
  • J. Chen, Z. Cheng, T. Quinn
  • Chemistry, Biology
    Journal of nuclear medicine : official publication, Society of Nuclear Medicine
  • 2001
The novel ReO-coordinated cyclic structure of DOTA-Re CCMSH contributes significantly to its enhanced tumor-targeting and renal clearance properties and makes DOTAReCCMSH an excellent candidate for melanoma radiodetection and radiotherapy.
Gallium-68-labeled DOTA-rhenium-cyclized alpha-melanocyte-stimulating hormone analog for imaging of malignant melanoma.
Targeted melanoma imaging and therapy with radiolabeled alpha-melanocyte stimulating hormone peptide analogues.
  • T. Quinn, X. Zhang, Y. Miao
  • Biology, Chemistry
    Giornale italiano di dermatologia e venereologia : organo ufficiale, Societa italiana di dermatologia e sifilografia
  • 2010
Strong pre-clinical imaging and therapy data highlight the clinical potential use of radiolabeled a-MSH peptides for melanoma imaging and treatment of disseminated disease.
Synthesis and biologic evaluation of 64Cu-labeled rhenium-cyclized alpha-MSH peptide analog using a cross-bridged cyclam chelator.
The data suggest the superior stability of the (64)Cu-CBTE2A moiety compared with (64]Cu-DOTA, making ( 64) Cu-CB TE2A-ReCCMSH(Arg(11)) an ideal candidate for the PET of malignant melanoma.
New small 99mTc-labeled peptides for HER2 receptor imaging.


Enhanced binding and inertness to dehalogenation of alpha-melanotropic peptides labeled using N-succinimidyl 3-iodobenzoate.
It is concluded that further evaluation of [Nle4,D-Phe7,Lys11-(125I)IBA]-alpha-MSH for targeting alpha- MSH receptors is warranted and that SIB may be a useful method for the radioiodination of peptides.
Preclinical evaluation of technetium-99m-labeled somatostatin receptor-binding peptides.
The high SSTR-binding affinity and high receptor-specific and saturable in vivo tumor uptake indicate that 99mTc-P587 and 99mGlucoheptonate-P829 are promising radiotracers for the clinical detection of S STR-expressing tumors and other tissues by 99m Tc gamma scintigraphy.
Biodistribution, pharmacokinetic, and imaging studies with 186Re-labeled NR-LU-10 whole antibody in LS174T colonic tumor-bearing mice.
The biodistribution, pharmacokinetic, and scintigraphic image results suggest that 186Re-labeled NR-LU-10 shows promise as a therapeutic agent for gastrointestinal cancer and in an experimental hepatic metastasis model.
Synthesis and characterization of rhenium-complexed alpha-melanotropin analogs.
A method of labeling peptides with rhenium using a natural amino acid chelating moiety could provide a general means of labeling bioactive peptide fragments that would simplify product purification and characterization.
Labeling cyclic glycoprotein IIb/IIIa receptor antagonists with 99mTc by the preformed chelate approach: effects of chelators on properties of [99mTc]chelator-peptide conjugates.
The 99mTc-labeled cyclic GPIIb/IIIa receptor antagonists were characterized by radio-HPLC (high-performance liquid chromatography); differences in lipophilicity of the [99MTc]chelator-peptide conjugate are attributable to the effects of both the cyclic peptide and the chelator.
4-Norleucine, 7-D-phenylalanine-alpha-melanocyte-stimulating hormone: a highly potent alpha-melanotropin with ultralong biological activity.
This Nle4, D-Phe7 synthetic analogue of alpha-MSH is a very porent melanotropin, 26 times as potent as alpha- MSH in the adenylate cyclase assay, and the resistance of the peptide to enzymatic degradation and its extraordinarily potent and prolonged biological activity should make this analogue ofalpha-MSh an important molecular probe for studying the melanotropic receptors of both normal and abnormal (melanoma) melanocytes.
Radiometal labeling of recombinant proteins by a genetically engineered minimal chelation site: technetium-99m coordination by single-chain Fv antibody fusion proteins through a C-terminal cysteinyl peptide.
  • A. George, F. Jamar, A. Peters
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1995
The 99mTc-labeled 741F8-1 sFv', specific for the c-erbB-2 tumor-associated antigen, is effective in imaging human ovarian carcinoma in a scid mouse tumor xenograft model.
[111In]‐DTPA‐labeled analogues of α‐melanocyte‐stimulating hormone for melanoma targeting: Receptor binding in vitro and in vivo
It is demonstrated that modification of the Lys10 side chain by DHP is a promising lead for new MSH radiopharmaceuticals for melanoma targeting.
Potent and prolonged acting cyclic lactam analogues of alpha-melanotropin: design based on molecular dynamics.
New insights are provided into the structural and conformational requirements of alpha-MSH and its analogues at two different types of pigment cell (melanocyte) receptors.