dimethyl bis(N-benzyloxycarbonyl)-L-homocystine | 255737-46-3

• 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: dimethyl bis(N-benzyloxycarbonyl)-L-homocystine
• 英文别名: (2S), 2-(benzyloxycarbonylamino), 4-[(3S), 3-benzyloxycarbonylamino, 3-methoxycarbonyl propyldisulfanyl]-butyric acid methyl ester；Cbz-Hcy(1)-OMe.Cbz-Hcy(1)-OMe；methyl (2S)-4-[[(3S)-4-methoxy-4-oxo-3-(phenylmethoxycarbonylamino)butyl]disulfanyl]-2-(phenylmethoxycarbonylamino)butanoate
• CAS: 255737-46-3
• 化学式: C₂₆H₃₂N₂O₈S₂
• 分子量: 564.681
• InChiKey: UPTDWTQGDYOJDG-VXKWHMMOSA-N

物化性质

• 沸点：
  717.8±60.0 °C(Predicted)
• 密度：
  1.279±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  38
• 可旋转键数：
  19
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  180
• 氢给体数：
  2
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  dimethyl bis(N-benzyloxycarbonyl)-L-homocystine 在 甲醇 、 氯 作用下， 以 四氯化碳 为溶剂， 以100%的产率得到(2S)-(benzyloxycarbonylamino)-4-chlorosulfonyl-butyric acid methyl ester
  参考文献：
  名称：

  Investigation of Subsite Preferences in Aminopeptidase A (EC 3.4.11.7) Led to the Design of the First Highly Potent and Selective Inhibitors of This Enzyme

  摘要：

  The study of the physiological roles of the membrane-bound zinc-aminopeptidase A (glutamyl aminopeptidase, EC 3.4.11.7) needs the design of efficient and selective inhibitors of this enzyme. An acute exploration of aminopeptidase A active site was performed by a combinatorial approach using (3-amino-2-mercapto-acyl)dipeptides able to sc its S-1, S-1', and S-2' subsites. This analysis confirmed that the S-1 subsite is optimally blocked by a glutamate or isosteric residues and demonstrated that the S-1' subsite is hydrophobic whereas the S-2' subsite recognizes preferentially negatively charged residues derived from aspartic acid. The optimization of these structural parameters led to the synthesis of nanomolar and subnanomolar inhibitors of aminopeptidase A such as H3N+CH(CH2CH2SO3-)CH(SH)CO-Ile-(3-COOH)Pro that exhibits a K-i of 0.87 nM. The best compounds were synthesized by a stereochemically controlled route. These first described highly potent inhibitors could allow studies about the role of physiological substrates of APA such as angiotensin II- and cholecystokinin CCK8 in the central nervous system.

  DOI：

  10.1021/jm9903040
• 作为产物：
  描述：

  N-苄氧羰基天冬氨酰胺甲基酯 在 亚硝酸特丁酯 、 benzyltriethylammonium tetrathiomolybdate 、 氯甲酸乙酯 作用下， 以 乙腈 为溶剂， 生成 dimethyl bis(N-benzyloxycarbonyl)-L-homocystine
  参考文献：
  名称：

  Utility of tetrathiomolybdate and tetraselenotungstate: efficient synthesis of cystine, selenocystine, and their higher homologues

  摘要：

  Efficient synthesis of cystine, selenocystine, and their higher homologues like homo and bishomo amino acid derivatives from natural amino acid derivatives using tetrathiomolybdate and tetraselenotungstate reagents under mild and neutral conditions is reported. The generality of the reaction has been studied by capping various groups to amino and carboxyl components of canonical amino acids. (C) 2003 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0040-4039(03)01222-x

文献信息

• Small molecule inhibitors of ghrelin O-acyltransferase
  申请人：Board of Regents, The University of Texas System

  公开号：US08013015B2

  公开（公告）日：2011-09-06

  Ghrelin O-acyltransferase (GOAT) is inhibited with designed small molecules. Methods comprise contacting the GOAT with an inhibitor and detecting a resultant inhibition.

  胃饥饿素O-酰基转移酶（GOAT）被设计的小分子抑制。方法包括将抑制剂与GOAT接触并检测所产生的抑制。
• Utility of tetrathiomolybdate and tetraselenotungstate: efficient synthesis of cystine, selenocystine, and their higher homologues
  作者：Ramakrishna G. Bhat、Emmanuel Porhiel、Vadivelu Saravanan、Srinivasan Chandrasekaran

  DOI：10.1016/s0040-4039(03)01222-x

  日期：2003.7

  Efficient synthesis of cystine, selenocystine, and their higher homologues like homo and bishomo amino acid derivatives from natural amino acid derivatives using tetrathiomolybdate and tetraselenotungstate reagents under mild and neutral conditions is reported. The generality of the reaction has been studied by capping various groups to amino and carboxyl components of canonical amino acids. (C) 2003 Elsevier Science Ltd. All rights reserved.
• Investigation of Subsite Preferences in Aminopeptidase A (EC 3.4.11.7) Led to the Design of the First Highly Potent and Selective Inhibitors of This Enzyme
  作者：Christelle David、Laurent Bischoff、Hervé Meudal、Aurélie Mothé、Nadia De Mota、Sophie DaNascimento、Catherine Llorens-Cortes、Marie-Claude Fournié-Zaluski、Bernard P. Roques

  DOI：10.1021/jm9903040

  日期：1999.12.1

  The study of the physiological roles of the membrane-bound zinc-aminopeptidase A (glutamyl aminopeptidase, EC 3.4.11.7) needs the design of efficient and selective inhibitors of this enzyme. An acute exploration of aminopeptidase A active site was performed by a combinatorial approach using (3-amino-2-mercapto-acyl)dipeptides able to sc its S-1, S-1', and S-2' subsites. This analysis confirmed that the S-1 subsite is optimally blocked by a glutamate or isosteric residues and demonstrated that the S-1' subsite is hydrophobic whereas the S-2' subsite recognizes preferentially negatively charged residues derived from aspartic acid. The optimization of these structural parameters led to the synthesis of nanomolar and subnanomolar inhibitors of aminopeptidase A such as H3N+CH(CH2CH2SO3-)CH(SH)CO-Ile-(3-COOH)Pro that exhibits a K-i of 0.87 nM. The best compounds were synthesized by a stereochemically controlled route. These first described highly potent inhibitors could allow studies about the role of physiological substrates of APA such as angiotensin II- and cholecystokinin CCK8 in the central nervous system.