H-hCys(Trt)-Phe(N-Me)-Tyr(tBu)-D-Trp-Lys(Boc)-Val-OH | 174900-00-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: H-hCys(Trt)-Phe(N-Me)-Tyr(tBu)-D-Trp-Lys(Boc)-Val-OH
• CAS: 174900-00-6
• 化学式: C₇₃H₉₀N₈O₁₀S
• 分子量: 1271.63
• InChiKey: SWEAKNQAAOXLKB-QZPHHHEASA-N

反应信息

• 作为反应物：
  描述：

  H-hCys(Trt)-Phe(N-Me)-Tyr(tBu)-D-Trp-Lys(Boc)-Val-OH 在 1-羟基苯并三唑 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 生成 {4-[(2S,5S,8S,11S,14S,17R)-11-Benzyl-14-(4-tert-butoxy-benzyl)-17-(1H-indol-3-ylmethyl)-5-isopropyl-10-methyl-3,6,9,12,15,18-hexaoxo-8-(2-tritylsulfanyl-ethyl)-1,4,7,10,13,16-hexaaza-cyclooctadec-2-yl]-butyl}-carbamic acid tert-butyl ester
  参考文献：
  名称：

  Somatostatin Receptor-Binding Peptides Labeled with Technetium-99m:  Chemistry and Initial Biological Studies

  摘要：

  The synthesis of peptides which possess a high affinity for the somatostatin receptor and contain a chelator for the radionuclide technetium-99m is described. The target compounds were designed such that they would form stable, oxotechnetium(V) chelate complexes in which the site of metal coordination was well defined and remote from the receptor-binding region. Oxorhenium(V) chelate complexes of these peptides were prepared as nonradioactive surrogates for the technetium complexes. Peptide oxorhenium complexes and Tc-99m complexes eluted closely upon HPLC analysis. The receptor-binding affinities of both the free and rhenium-coordinated species were measured in vitro. The binding affinities of the free peptides (K-i's in the 0.25-10 nM range) compared favorably with [DTPA]octreotide (K-i = 1.6 nM), which, as the indium-lll complex, is already approved for somatostatin receptor (SSTR)-expressing tumor imaging in the United States and Europe. Furthermore, the rhenium-coordinated peptides had binding affinities which, in many cases, were higher than those of the corresponding free peptides, with several complexes having a K-i's of 0.1 nM. Some of the more potent SSTR-binding peptides were labeled with technetium-99m and assessed in an in vivo study with tumor-bearing rats. The Tc-99m-labeled peptides prepared in this study should be useful as SSTR-expressing tumor-imaging agents due to their high SSTR-binding affinities, ease of preparation, and, because they are low molecular weight peptides, expected pharmacokinetics characterized by rapid tracer excretion from the body resulting in high-contrast images.

  DOI：

  10.1021/jm950111m
• 作为产物：
  描述：

  H-hCys(Trt)-Phe(N-Me)-Tyr(tBu)-D-Trp-Lys(Boc)-Val-OMe 在 lithium hydroxide 作用下， 以 四氢呋喃 为溶剂， 反应 4.0h， 生成 H-hCys(Trt)-Phe(N-Me)-Tyr(tBu)-D-Trp-Lys(Boc)-Val-OH
  参考文献：
  名称：

  Somatostatin Receptor-Binding Peptides Labeled with Technetium-99m:  Chemistry and Initial Biological Studies

  摘要：

  The synthesis of peptides which possess a high affinity for the somatostatin receptor and contain a chelator for the radionuclide technetium-99m is described. The target compounds were designed such that they would form stable, oxotechnetium(V) chelate complexes in which the site of metal coordination was well defined and remote from the receptor-binding region. Oxorhenium(V) chelate complexes of these peptides were prepared as nonradioactive surrogates for the technetium complexes. Peptide oxorhenium complexes and Tc-99m complexes eluted closely upon HPLC analysis. The receptor-binding affinities of both the free and rhenium-coordinated species were measured in vitro. The binding affinities of the free peptides (K-i's in the 0.25-10 nM range) compared favorably with [DTPA]octreotide (K-i = 1.6 nM), which, as the indium-lll complex, is already approved for somatostatin receptor (SSTR)-expressing tumor imaging in the United States and Europe. Furthermore, the rhenium-coordinated peptides had binding affinities which, in many cases, were higher than those of the corresponding free peptides, with several complexes having a K-i's of 0.1 nM. Some of the more potent SSTR-binding peptides were labeled with technetium-99m and assessed in an in vivo study with tumor-bearing rats. The Tc-99m-labeled peptides prepared in this study should be useful as SSTR-expressing tumor-imaging agents due to their high SSTR-binding affinities, ease of preparation, and, because they are low molecular weight peptides, expected pharmacokinetics characterized by rapid tracer excretion from the body resulting in high-contrast images.

  DOI：

  10.1021/jm950111m