o-NBS-Ala-OtBu | 247167-06-2

• 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: o-NBS-Ala-OtBu
• 英文别名: tert-butyl (2S)-2-[(2-nitrophenyl)sulfonylamino]propanoate
• CAS: 247167-06-2
• 化学式: C₁₃H₁₈N₂O₆S
• 分子量: 330.362
• InChiKey: HAQGLJCPAKAEFX-VIFPVBQESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2
• 重原子数：
  22
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  127
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  o-NBS-Ala-OtBu 在 potassium carbonate 、 苯硫酚 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 tert-butyl (S)-2-(Allylamino)propanoate
  参考文献：
  名称：

  Rational design of an orthosteric regulator of hIAPP aggregation

  摘要：

  可以阻断hIAPP有毒寡聚体形成但不阻止纤维形成的化合物已经根据螺旋聚集机制进行了合理设计。

  DOI：

  10.1039/c4cc06739h
• 作为产物：
  描述：

  L-丙氨酸叔丁酯盐酸盐 在 potassium carbonate 、 三乙胺 作用下， 以 二氯甲烷 、 水 为溶剂， 生成 o-NBS-Ala-OtBu
  参考文献：
  名称：

  Rational design of an orthosteric regulator of hIAPP aggregation

  摘要：

  可以阻断hIAPP有毒寡聚体形成但不阻止纤维形成的化合物已经根据螺旋聚集机制进行了合理设计。

  DOI：

  10.1039/c4cc06739h

文献信息

• Methods for preparing internally constrained peptides and peptidomimetics
  申请人：New York University

  公开号：US09221871B2

  公开（公告）日：2015-12-29

  The present invention relates to a method for preparing a peptide having a stable, internally constrained alpha-helical, beta-sheet/beta-turn, 310-helical, or pi-helical region and a method of stabilizing an alpha-helical, beta-sheet/beta-turn, 310-helical, or pi-helical region within a peptide structure. The resulting peptides and methods of using them are also disclosed.

  本发明涉及一种制备具有稳定的内部约束α-螺旋、β-折叠/β-转角、310-螺旋或π-螺旋区域的肽的方法，以及稳定肽结构内α-螺旋、β-折叠/β-转角、310-螺旋或π-螺旋区域的方法。还公开了所得到的肽及其使用方法。
• Mitsunobu glycosylation of nitrobenzenesulfonamides: Novel route to amadori rearrangement products
  作者：John J. Turner、Niels Wilschut、Herman S. Overkleeft、Werner Klaffke、Gijs A. van der Marel、Jacques H. van Boom

  DOI：10.1016/s0040-4039(99)01452-5

  日期：1999.9

  condensed under Mitsunobu conditions with 2,3,4,6-tetra-O-acetyl-d-glucose to afford the fully protected glucosylamines in excellent yield. Upon total deprotection, these compounds rearranged to provide the corresponding Amadori products in good overall yield.

  在Mitsunobu条件下，将氨基酸衍生的2-硝基苯磺酰胺与2,3,4,6-四-O-乙酰基-d-葡萄糖成功缩合，从而以极佳的收率得到完全保护的葡糖胺。在完全脱保护后，这些化合物重新排列以提供具有良好总收率的相应的Amadori产物。
• Novel Reversed Chain Modified Oligopeptides via Sequential α-<i>N</i>-Mitsunobu Condensation of a Functionalized C-glycoside
  作者：John J. Turner、Friso D. Sikkema、Kees Erkelens、Gijs A. van der Marel、Herman S. Overkleeft、Jacques H. van Boom、Mark Overhand

  DOI：10.1246/cl.2004.468

  日期：2004.4

  The synthesis of a novel reversed chain modified oligopeptide via sequential α-N-Mitsunobu condensation reactions on a C-glycoside with amino acid derived nitrobenzenesulfonamides is described. Str...

  描述了通过连续 α-N-Mitsunobu 缩合反应在 C-糖苷上与氨基酸衍生的硝基苯磺酰胺合成新型反链修饰寡肽。强...
• Synthesis of novel amino acid carbohydrate hybrids via Mitsunobu glycosylation of nitrobenzenesulfonamides
  作者：John J. Turner、Dmitri V. Filippov、Mark Overhand、Gijs A. van der Marel、Jacques H. van Boom

  DOI：10.1016/s0040-4039(01)01062-0

  日期：2001.8

  Amino acid derived 2-nitrobenzenesulfonamides were successfully condensed under Mitsunobu conditions with the primary alcohol of various saccharide and nucleoside derivatives to furnish the fully protected hybrids in excellent yield. One such hybrid was incorporated into a short peptide sequence in good overall yield. (C) 2001 Elsevier Science Ltd. All rights reserved.
• A Highly Stable Short α-Helix Constrained by a Main-Chain Hydrogen-Bond Surrogate
  作者：Ross N. Chapman、Gianluca Dimartino、Paramjit S. Arora

  DOI：10.1021/ja0466659

  日期：2004.10.1

  Herein we describe a strategy for the preparation of artificial alpha-helices involving replacement of one of the main-chain hydrogen bonds with a covalent linkage. To mimic the C=O...H-N hydrogen bond as closely as possible, we envisioned a covalent bond of the type C=X-Y-N, where X and Y are two carbon atoms connected through an olefin metathesis reaction. Our results demonstrate that the replacement of a hydrogen bond between the i and i + 4 residues at the N-terminus of a short peptide with a carbon-carbon bond results in a highly stable constrained alpha-helix at physiological conditions as indicated by CD and NMR spectroscopies. The advantage of this strategy is that it allows access to short alpha-helices with strict preservation of molecular recognition surfaces required for biomolecular interactions.