N^α-t-Boc-S-(carbomethoxysulfenyl)-L-cysteine | 45234-12-6

• 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: N^α-t-Boc-S-(carbomethoxysulfenyl)-L-cysteine
• 英文别名: Boc-Cys(Scm)-OH；(2R)-3-(methoxycarbonyldisulfanyl)-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid
• CAS: 45234-12-6
• 化学式: C₁₀H₁₇NO₆S₂
• 分子量: 311.38
• InChiKey: BIJLJADFPYFTJY-LURJTMIESA-N

物化性质

• 密度：
  1.340±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.11
• 重原子数：
  19.0
• 可旋转键数：
  5.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.7
• 拓扑面积：
  101.93
• 氢给体数：
  2.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  BOC-甘氨酸 、 N-Boc-L-缬氨酸 、 N^α-t-Boc-S-(carbomethoxysulfenyl)-L-cysteine 、 溶剂黄146 生成 Ac-Gly-Cys(Scm)-Val-NH2
  参考文献：
  名称：

  A new protecting group for the sulfhydryl function of cysteine

  摘要：

  DOI：

  10.1021/jo00262a051
• 作为产物：
  描述：

  methyl (1,1,3-trioxo-1,2-benzothiazol-2-yl)sulfanylformate 、 S-乙酰胺基甲基-N-叔丁氧羰基-L-半胱氨酸 生成 N^α-t-Boc-S-(carbomethoxysulfenyl)-L-cysteine
  参考文献：
  名称：

  KAUFMANN, K. -D.;KUNZEK, H.;WINTER, R.

  摘要：

  DOI：

文献信息

• Synthesis of a 39-peptide and a 25-peptide by thiol capture ligations: observation of a 40-fold rate acceleration of the intramolecular O,N-acyl-transfer reaction between peptide fragments bearing only cysteine protective groups
  作者：D. S. Kemp、Robert I. Carey

  DOI：10.1021/jo00060a043

  日期：1993.4

  In this paper we report the syntheses of the 39-peptide C(Acm)LNELDADEQADL-CESLHDHADEunderbar-LYRSCLARFGDDGENL, 1, and of the 25-peptide C(Acm)LNELDADEQADL-CLARFGDDGENLunberbar, 2, by means of thiol capture ligations using precursor peptides bearing blocking groups only on cysteine residues. The ligations were made in each case at the underlined cysteine, cleanly and in high yield. For each of the above syntheses, an acidolytically deblocked 13-peptide dibenzofuranyl ester, 6-[C(Acm)LNELDADEQADLeucinyloxy]-4-mercaptodibenzofuran, 3, was prepared in pure form in 52% overall yield through three stages: (1) stepwise synthesis on a solid-phase resin loaded with the dibenzofuran template, (2) acidolytic removal of the tert-butyl esters of the resin-bound peptide, and (3) preparative cleavage of the deblocked peptidyloxydibenzofuran ester from the resin. In the case of both the 39-peptide and the 25-peptide, significant rate enhancements were seen for the O,N-acyl-transfer step of the thiol capture sequence when both the N-terminal and C-terminal fragments had been previously side-chain deblocked, in comparison with the cases when only the C-terminal fragment had been side-chain deblocked. In the 13-peptide + 12-peptide ligation to form the 25-peptide 2, a t1/2 = 5 min was seen for the leucine-cysteine amide bond-forming reaction. A model leucine-cysteine O,N-acyl transfer as well as leucine-cysteine O,N-acyl transfers between protected peptide fragments, however, showed the expected t1/2 = 4h. Rationalization of this observed 40-fold rate enhancement is offered that identifies the aspartic acid side chain carboxylate, 12 residues in sequence from the N-terminus and penultimate to the amide ligation site, as a possible intramolecular general base catalyst for the proton-transfer step during the O,N-acyl transfer.
• CARDINAUX, FRANCOIS;PIESS, JANOS;BUCK, ROBERT HELMUT
  作者：CARDINAUX, FRANCOIS、PIESS, JANOS、BUCK, ROBERT HELMUT

  DOI：——

  日期：——