H-Cys(MBzl)-OBzl*Tos-OH | 54649-52-4

• 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-Cys(MBzl)-OBzl*Tos-OH
• 英文别名: H-Cys(MBzl)-OBzl*TosOH
• CAS: 54649-52-4
• 化学式: C₇H₈O₃S*C₁₈H₂₁NO₃S
• 分子量: 503.64
• InChiKey: RPMBMGWIXBTCQD-LMOVPXPDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.24
• 重原子数：
  34.0
• 可旋转键数：
  9.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.24
• 拓扑面积：
  115.92
• 氢给体数：
  2.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  H-Cys(MBzl)-OBzl*Tos-OH 在 1-羟基苯并三唑 、 苯甲醚 、 三乙胺 、 N,N'-二环己基碳二亚胺 、 三氟乙酸 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 1.17h， 生成 Boc-Cys(MBzl)-Ile-Cys(MBzl)-OBzl
  参考文献：
  名称：

  Amino acids and peptides. VIII. Synthesis of a hexacosapeptide corresponding to the C-terminal sequence 36-61 of human metallothionein II (hMT II) and determination of its heavy metal binding activity.

  摘要：

  使用叠氮化物程序通过片段缩合法合成了对应于人肝金属硫蛋白(hMT II)的残基36-61的C端六肽。通过甲磺酸（MSA）法或氟化氢（HF）法去除保护基，得到所需的肽。通过测量紫外区（200-260 nm）的吸光度作为重金属浓度的函数并通过凝胶过滤方法检查该肽与 Cd 和 Zn 的结合能力。该肽的重金属结合行为与硫因非常相似。

  DOI：

  10.1248/cpb.31.1885

文献信息

• Amino acids and peptides. IX. Synthesis of cysteine-containing peptide fragments related to human hepatic metallothionein II (hMT II) and determination of their heavy metal-binding properties.
  作者：NORIYA OHTA、YOSHIO OKADA、KEIICHI TANAKA

  DOI：10.1248/cpb.31.3094

  日期：——

  Eight kinds of cysteine-containing peptides related to human hepatic metallothionein were synthesized by conventional methods. The metal-binding properties of these peptides with Zn2+ and Cd2+ were indicated by an increase of ultraviolet absorbance resulting from mercaptide formation. The Cd-binding activities of various peptides obtained here were assessed by measuring the increase in absorbance of mercaptide at 250 nm as a function of the concentration of Cd. The binding abilities of the peptides with Cd differed substancially.

  采用传统方法合成了八种与人类肝脏金属硫蛋白相关的含半胱氨酸肽。这些肽与 Zn2+ 和 Cd2+ 的金属结合特性是通过巯基的形成导致紫外吸光度的增加来显示的。通过测量 250 纳米波长处硫醇吸光度的增加与镉浓度的函数关系，评估了在此获得的各种多肽的镉结合活性。肽与镉的结合能力有很大差异。
• Amino acids and peptides. XXIV. Synthesis of Neurospora crassa metallothionein and related cysteine-containing peptides and examination of their heavy metal-binding properties.
  作者：Yoshio OKADA、Yutaka MATSUNO、Yasuhiro NSHIYAMA、Yuko TSUDA、Shin IGUCHI、Kyong-Son MIN、Satomi ONOSAKA、Keiichi TANAKA

  DOI：10.1248/cpb.37.2322

  日期：——

  corresponding to the entire amino acid sequence of Neurospora crassa metallothionein and several related cysteine-containing peptides were synthesized by the conventional solution method and their heavy metal-binding properties were examined. The Cu2+- or Cu+-binding properties of the various peptides were similar to each other, whereas the Cd2+-binding properties of these peptides were fairly structure-dependent

  通过常规溶液法合成了与芥菜神经孢菌金属硫蛋白的整个氨基酸序列相对应的五肽和几种相关的含半胱氨酸的肽，并检查了它们的重金属结合特性。各种肽的Cu2 +或Cu +结合性质彼此相似，而这些肽的Cd2 +结合性质是相当结构依赖性的。
• Amino acids and peptides. XIII. Synthesis of a nonacosapeptide corresponding to the N-terminal sequence 1-29 (.BETA.-fragment) of human liver metallothionein II (hMT II) and its heavy metal-binding properties.
  作者：YOSHIO OKADA、NORIYA OHTA、SHIN IGUCHI、YUKO TSUDA、HIDEAKI SASAKI、TOKUJIRO KITAGAWA、MASAMI YAGYU、KYON-SON MIN、SATOMI ONOSAKA、KEIICHI TANAKA

  DOI：10.1248/cpb.34.986

  日期：——

  A nonacosapeptide corresponding to the N-terminal sequence 1-29 (β-fragment) of human liver metallothionein II (hMT II) was synthesized by the azide coupling of five peptide fragments [1, 2, 4, 6 and 8], followed by HF deprotection and its heavy metal-binding properties were examined. It was revealed that the Cd-binding ability of the synthetic β-fragment as well as synthetic α-fragment corresponding to the C-terminal sequence 30-61 of hMT II was stronger than that of native rat thionein. Moreover, it was found that both the α-and β-fragments bound preferentially to Cu ions rather than Cd ions.

  通过叠氮偶联五种肽段[1、2、4、6和8]，然后进行高频脱保护，合成了对应于人肝金属硫蛋白II（hMT II）N端序列1-29（β-片段）的非酰肽，并考察了其重金属结合特性。结果表明，与 hMT II C 端序列 30-61 相应的合成 β 片段和合成 α 片段的镉结合能力强于原生大鼠硫蛋白。此外，研究还发现α-片段和β-片段都优先与铜离子而不是镉离子结合。