Fmoc-Thr(tBu)-NHBn | 929294-62-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: Fmoc-Thr(tBu)-NHBn
• 英文别名: 9H-fluoren-9-ylmethyl N-[(2S,3R)-1-(benzylamino)-3-[(2-methylpropan-2-yl)oxy]-1-oxobutan-2-yl]carbamate
• CAS: 929294-62-2
• 化学式: C₃₀H₃₄N₂O₄
• 分子量: 486.611
• InChiKey: VIONKKLTFUCEBJ-HRFSGMKKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.2
• 重原子数：
  36
• 可旋转键数：
  10
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  76.7
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Fmoc-Thr(tBu)-NHBn 在 吡啶 、 三氟乙酸 作用下， 生成 Fmoc-Thr(CO2-nitrophenyl)-NHBn
  参考文献：
  名称：

  Solid-phase synthesis of Stat3 inhibitors incorporating O-carbamoylserine and O-carbamoylthreonine as glutamine mimics

  摘要：

  O-Carbamoyiserine and O-carbamoylthreonine are glutamine analogues that were incorporated into a Stat3 inhibitory peptide to probe the requirements of Gin at the pY+3 position. Fmoc-Ser-NHBn and Fmoc-Thr-NHBn were converted to nitrophenyl carbonates and were attached to Rink resin via a side-chain carbamate linkage. After assembly of the peptide, acid treatment resulted in O-carbamoylserine and O-carbamoylthreonine-containing peptides. The order of affinity for Stat3 was Gin > Ser (CONH2) > Thr(CONH2) suggesting a relatively tight binding pocket for the side chain of glutamine. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2006.10.099
• 作为产物：
  描述：

  Fmoc-O-叔丁基-L-苏氨酸 、 苄胺 在 N,N-二异丙基乙胺 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.58h， 以1.2 g的产率得到Fmoc-Thr(tBu)-NHBn
  参考文献：
  名称：

  未受保护肽的氮丙啶介导的连接和位点特异性修饰

  摘要：

  报道了通过未保护的肽硫代酸和 NH 氮丙啶-2-羰基肽的 Cu(II) 促进偶联合成含氮丙啶肽。所得 N-酰化氮丙啶-2-羰基肽的独特反应性促进了它们随后的区域选择性和立体选择性亲核开环，以产生在连接位点被特异性修饰的未保护肽。氮丙啶介导的肽连接概念以 H(2)O 作为亲核试剂为例，产生 Xaa-Thr 连接（其中 Xaa 可以是差向异构和受阻氨基酸）。整个过程与各种未受保护的氨基酸官能团兼容，最显着的是 N 端和 Lys 侧链胺。

  DOI：

  10.1021/ja207133t

文献信息

• Aziridine mediated native chemical ligation
  申请人：Washington State University

  公开号：US08981049B2

  公开（公告）日：2015-03-17

  Improved methods of native chemical ligation are provided. The methods involve reacting a thioacid (e.g. a peptide thioacid) with an aziridinyl compound (e.g. an aziridinyl peptide) under mild conditions without the use of protecting groups, and without requiring that a cysteine residue be present in the ligation product. Initial coupling of the thioacid and the aziridinyl compound yields a ligation product which contains an aziridinyl ring. Subsequent opening of the aziridinyl ring (e.g. via a nucleophilic attack) produces a linearized and modified ligation product.

  提供了改进的天然化学连接方法。该方法涉及在温和条件下反应硫酸（例如肽硫酸）和环氧丙烷化合物（例如环氧丙烷肽），无需保护基，且不需要连接产物中存在半胱氨酸残基。硫酸和环氧丙烷化合物的初始偶联产生含有环氧丙烷环的连接产物。随后通过亲核攻击等方式打开环氧丙烷环，产生线性化和改性的连接产物。
• VERSATILE NATIVE CHEMICAL LIGATION TECHNOLOGIES
  申请人：Washington State University

  公开号：US20140213758A1

  公开（公告）日：2014-07-31

  Novel methods of native chemical ligation are provided. The methods involve reacting a thioacid (e.g. a peptide thioacid) with an aziridinyl compound (e.g. an aziridinyl peptide) or glycosylamine under mild conditions without the use of protecting groups, and without requiring that a cysteine residue be present in the ligation product. Initial coupling of the thioacid and the aziridinyl compound yields a ligation product containing an aziridinyl ring. Optional subsequent opening of the aziridinyl ring (e.g. via a nucleophilic attack) produces a linearized and modified ligation product. Coupling of a peptide thioacid and glycosylamine yields a glycosylated peptide.

  提供一种原生化学连接的新方法。该方法涉及在温和条件下反应硫代酸（例如肽硫代酸）与环氧丙烷化合物（例如环氧丙烷肽）或者葡萄糖氨基化合物，无需使用保护基，并且不需要在连接产物中存在半胱氨酸残基。硫代酸和环氧丙烷化合物的初始偶联产生含有环氧丙烷环的连接产物。选择性地通过环氧丙烷环的后续开放（例如通过亲核攻击）可产生线性化和改性的连接产物。肽硫代酸和葡萄糖氨基化合物的偶联产生糖基化肽。
• Versatile native chemical ligation technologies
  申请人：Washington State University

  公开号：US09145440B2

  公开（公告）日：2015-09-29

  Novel methods of native chemical ligation are provided. The methods involve reacting a thioacid (e.g. a peptide thioacid) with an aziridinyl compound (e.g. an aziridinyl peptide) or glycosylamine under mild conditions without the use of protecting groups, and without requiring that a cysteine residue be present in the ligation product. Initial coupling of the thioacid and the aziridinyl compound yields a ligation product containing an aziridinyl ring. Optional subsequent opening of the aziridinyl ring (e.g. via a nucleophilic attack) produces a linearized and modified ligation product. Coupling of a peptide thioacid and glycosylamine yields a glycosylated peptide.

  提供了一种新的天然化学连接方法。该方法涉及在温和条件下，不使用保护基，也不需要连接产物中存在半胱氨酸残基的情况下，将硫酸（例如肽硫酸）与环氧丙烷化合物（例如环氧丙烷肽）或氨基葡萄糖酰胺反应。硫酸和环氧丙烷化合物的初始偶联产生一个含有环氧丙烷环的连接产物。可选的后续开放环氧丙烷环（例如通过亲核攻击）产生线性化和修饰的连接产物。肽硫酸和氨基葡萄糖酰胺的偶联产生一个糖基化肽。
• AZIRIDINE MEDIATED NATIVE CHEMICAL LIGATION
  申请人：Washington State University

  公开号：US20130131311A1

  公开（公告）日：2013-05-23

  Improved methods of native chemical ligation are provided. The methods involve reacting a thioacid (e.g. a peptide thioacid) with an aziridinyl compound (e.g. an aziridinyl peptide) under mild conditions without the use of protecting groups, and without requiring that a cysteine residue be present in the ligation product. Initial coupling of the thioacid and the aziridinyl compound yields a ligation product which contains an aziridinyl ring. Subsequent opening of the aziridinyl ring (e.g. via a nucleophilic attack) produces a linearized and modified ligation product.

  提供了改进的天然化学连接方法。该方法涉及在温和条件下，无需使用保护基，也无需要求连接产物中存在半胱氨酸残基，将硫酸（例如肽硫酸）与环氧丙烷化合物（例如环氧丙烷肽）反应。硫酸和环氧丙烷化合物的初始偶联产生一个含有环氧丙烷环的连接产物。随后通过亲核攻击等方式打开环氧丙烷环，产生线性化和改性的连接产物。
• US8981049B2
  申请人：——

  公开号：US8981049B2

  公开（公告）日：2015-03-17