The safety and pharmacokinetics in adult subjects of an intravenously administered 99mTc-labeled 17 amino acid peptide (CYT-379)

Ben‐Haim, Simona; Kahn, Daniel; Weiner, George J.; Madsen, Mark T.; Williams, Cynthia M.; Clarke‐Pearson, Daniel L.; Coleman, Robert E.; Maguire, Robert T.

doi:10.1016/0969-8051(94)90001-9

Cited by 12 publications

(5 citation statements)

References 19 publications

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“…Other 99m Tc-labeled receptor ligands for thrombus imaging include TP-1300 (CSVTCR), snake venom peptides, , and MP-2026 (Thromboscan), which is an N 3 S-conjugated RGD peptidomimetic analogue. TP-1300 was modified with an N 4 Gly−Ala−Gly−Gly binding group for 99m Tc-labeling and an Aba (2,4-diaminobutanoic acid) linker.…”

Section: A Thrombus Imagingmentioning

confidence: 99%

“…The low sensitivity and accuracy of 99m Tc-CYT-379 was also attributed to its slow clearance from blood plasma and the partial heptabilary excretion. 390 Other 99m Tc-labeled receptor ligands for thrombus imaging include TP-1300 (CSVTCR), 391 snake venom peptides, 392,393 and MP-2026 (Thromboscan), 394 which is an N 3 S-conjugated RGD peptidomimetic analogue. TP-1300 was modified with an N 4 Gly-Ala-Gly-Gly binding group for 99m Tc-labeling and an Aba (2,4diaminobutanoic acid) linker.…”

Section: A Thrombus Imagingmentioning

confidence: 99%

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^99mTc-Labeled Small Peptides as Diagnostic Radiopharmaceuticals

1999

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Section: A Thrombus Imagingmentioning

confidence: 99%

Section: A Thrombus Imagingmentioning

confidence: 99%

^99mTc-Labeled Small Peptides as Diagnostic Radiopharmaceuticals

1999

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“…We are considering non-thiol-containing amino acids or small peptides as potential BFCAs, since they avoid the thiol protection step that reduces labeling efficiency and the specific activity of the labeled biomolecule. The literature on Re(V) complexes with amino acids other than the thiolate-containing cysteine or penicillamine is limited to the complex with the N 4 donor system Gly-Ala-Gly-Gly, ionic compounds of the type [ReO(dien-H)(aa)] + , where dien-H is deprotonated diethylenetriamine and aa is glycine, alanine, valine, leucine, or proline, the ReOX 2 (his) complexes (X = Cl, Br) containing N,N,O-tridentate histidine prepared by our research groups, and the recently reported species with the tetradentate N 3 O ligand 3-hydroxy-4-[2-(2‘-pyridinecarboxamido)acetylamino]benzoic acid …”

Section: Introductionmentioning

confidence: 99%

Binding of the Oxo−Rhenium(V) Core to Methionine and to N-Terminal Histidine Dipeptides

2004

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The ReOX(2)(met) compounds (X = Cl, Br) adopt a distorted octahedral structure in which a carboxylato oxygen lies trans to the Re=O bond, whereas the equatorial plane is occupied by two cis halides, an NH(2), and an SCH(3) group. Coordination of the SCH(3) unit creates an asymmetric center, leading to two diastereoisomers. X-ray diffraction studies reveal that the crystals of ReOBr(2)(d,l-met).1/2H(2)O and ReOBr(2)(d,l-met).1/2CH(3)OH contain only the syn isomer (S-CH(3) bond on the side of the Re=O bond), whereas ReOCl(2)(d-met) and ReOCl(2)(d,l-met) consist of the pure anti isomer. (1)H NMR spectroscopy shows that both isomers coexist in equilibrium in acetone (anti/syn ratio = 1:1 for X = Br, 3:1 for X = Cl). Exchange between these two isomers is fast above room temperature, but it slows down below 0 degrees C, and the sharp second-order spectra of both isomers at -20 degrees C were fully assigned. The coupling constants are consistent with the solid-state conformations being retained in solution. Complexes of the type [ReOX(2)(His-aa)]X (X = Cl, Br) are isolated with the dipeptides His-aa (aa = Gly, Ala, Leu, and Phe). X-ray diffraction work on [ReOBr(2)(His-Ala)]Br reveals the presence of distorted octahedral cations containing the Re=O(3+) core and a dipeptide coordinated through the histidine residue via the imidazole nitrogen, the terminal amino group, and the amide oxygen, the site trans to the Re=O bond being occupied by the oxygen. The alanine residue is ended by a protonated carboxylic group that does not participate in the coordination. The constant pattern of the(1)H NMR signals for the protons in the histidine residue confirms that the various dipeptides adopt a similar binding mode, consistent with the solid-state structure being retained in CD(3)OD solution.

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“…Thiol-containing peptides present a serious inconvenience in radiopharmacy: they are unstable in the free form and must be protected during storage, leading to a reduced labeling efficiency and specific activity of the Tc-labeled biomolecule. For an N 4 donor set, such as the Gly-Ala-Gly-Gly tetrapeptide, this protection step is unnecessary. We are considering histidine-containing peptides, which can be stored in a nonprotected form, as alternative ways of labeling the biological molecules with Tc or Re radionuclei.…”

Section: Introductionmentioning

confidence: 99%

Oxorhenium(V) Complexes with the Non-Sulfur-Containing Amino Acid Histidine

2002

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Equivalent amounts of ReOX(3)(OPPh(3))(Me(2)S) (where X = Cl, Br) and L-histidine (L-hisH) in acetonitrile yield ReOX(2)(L-his), in which the amino acid monoanion is N,N,O-tridentate. X-ray diffraction work on both compounds shows that the three donors occupy a face in a distorted octahedron and the carboxylate oxygen is coordinated trans to the Re=O bond. The 2:1 complex [ReO(L-his)(2)]I is obtained by reacting 2 equiv of L-histidine with ReO(2)I(PPh(3))(2) in methanol in the presence of NaOCH(3). (1)H NMR spectroscopy indicates that these complexes contain one N,N,O-tridentate histidine anion coordinated as above and one N,N-bidentate histidine anion, whose carboxylate group is free. By refluxing ReOX(2)(L-his) in methanol, the carboxylic groups esterify and two octahedral units condense into an oxo-bridged dinuclear complex [ReOX(2)(L-hisMe)](2)O containing N,N-bidentate histidine methyl ester. The O=Re-O-Re=O backbone is approximately linear, and the two ReOX(2)(L-hisMe) units are related by a 2-fold axis through the central oxygen. Crystals of [ReOBr(2)(L-hisMe)](2)O consist of an ordered phase containing two of the possible diastereoisomers in a 1:1 ratio. (1)H NMR spectra of these crystals include two sets of signals, consistent with the presence of two isomers with C(2) symmetry, and the spectra of the nonrecrystallized material confirm that these are the only two isomers formed.

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The safety and pharmacokinetics in adult subjects of an intravenously administered 99mTc-labeled 17 amino acid peptide (CYT-379)

Cited by 12 publications

References 19 publications

^99mTc-Labeled Small Peptides as Diagnostic Radiopharmaceuticals

^99mTc-Labeled Small Peptides as Diagnostic Radiopharmaceuticals

Binding of the Oxo−Rhenium(V) Core to Methionine and to N-Terminal Histidine Dipeptides

Oxorhenium(V) Complexes with the Non-Sulfur-Containing Amino Acid Histidine

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