L-allo-Thr(OBn) | 88357-80-6

• 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: L-allo-Thr(OBn)
• 英文别名: Benzyl (2s,3s)-2-amino-3-hydroxybutanoate
• CAS: 88357-80-6
• 化学式: C₁₁H₁₅NO₃
• 分子量: 209.245
• InChiKey: IHRYAQVOEVWURS-WPRPVWTQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.5
• 重原子数：
  15
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.36
• 拓扑面积：
  72.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  L-allo-Thr(OBn) 在 吡啶 、 氯化亚砜 、 sodium cyanoborohydride 、 溶剂黄146 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 12.0h， 生成 (4S,5S)-3-(4-Methoxy-benzyl)-5-methyl-2-oxo-2λ⁴-[1,2,3]oxathiazolidine-4-carboxylic acid benzyl ester
  参考文献：
  名称：

  Application of Serine- and Threonine-Derived Cyclic Sulfamidates for the Preparation of S-Linked Glycosyl Amino Acids in Solution- and Solid-Phase Peptide Synthesis

  摘要：

  Cyclic sulfamidates were synthesized in 60% yield from L-serine and allo-L-threonine, respectively. These sulfamidates reacted with a variety of unprotected 1-thio sugars in aqueous bicarbonate buffer (pH 8) to afford the corresponding S-linked serine- and threonine-glycosyl amino acids with good diastereo-selectivity (greater than or equal to97%) after hydrolysis of the A sulfates. The serine-derived sulfamidate was incorporated into a simple dlipeptide to generate a reactive dipeptide substrate that underwent chemoselective ligation with a 1-thio sugar to afford an S-linked glycopeptide. This sulfamidate was also incorporated into a peptide on a solid support in conjunction with solid-phase peptide synthesis. Chemoselective ligation of a 1-thio sugar with the cyclic sulfamidate was achieved on the solid support, followed by removal of the N-sulfate. Finally, the peptide chain of the resulting support-bound S-linked glycopeptide was extended using standard peptide synthesis procedures.

  DOI：

  10.1021/ja011932l
• 作为产物：
  描述：

  Boc-L-allo-Thr-OBn 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 2.0h， 生成 L-allo-Thr(OBn)
  参考文献：
  名称：

  Application of Serine- and Threonine-Derived Cyclic Sulfamidates for the Preparation of S-Linked Glycosyl Amino Acids in Solution- and Solid-Phase Peptide Synthesis

  摘要：

  Cyclic sulfamidates were synthesized in 60% yield from L-serine and allo-L-threonine, respectively. These sulfamidates reacted with a variety of unprotected 1-thio sugars in aqueous bicarbonate buffer (pH 8) to afford the corresponding S-linked serine- and threonine-glycosyl amino acids with good diastereo-selectivity (greater than or equal to97%) after hydrolysis of the A sulfates. The serine-derived sulfamidate was incorporated into a simple dlipeptide to generate a reactive dipeptide substrate that underwent chemoselective ligation with a 1-thio sugar to afford an S-linked glycopeptide. This sulfamidate was also incorporated into a peptide on a solid support in conjunction with solid-phase peptide synthesis. Chemoselective ligation of a 1-thio sugar with the cyclic sulfamidate was achieved on the solid support, followed by removal of the N-sulfate. Finally, the peptide chain of the resulting support-bound S-linked glycopeptide was extended using standard peptide synthesis procedures.

  DOI：

  10.1021/ja011932l

文献信息

• LYSOBACTIN AMIDES
  申请人：VON NUSSBAUM Franz

  公开号：US20090203582A1

  公开（公告）日：2009-08-13

  The invention relates to lysobactin amides and methods for their preparation, as well as their use for manufacturing medicaments for the treatment and/or prophylaxis of diseases, in particular bacterial infectious diseases.

  这项发明涉及赖氨酸胞素酰胺及其制备方法，以及它们用于制造治疗和/或预防疾病，特别是细菌感染性疾病的药物的用途。
• METHOD FOR PREPARING LYSOBACTIN DERIVATIVES
  申请人：VON NUSSBAUM Franz

  公开号：US20090163696A1

  公开（公告）日：2009-06-25

  Method for preparing cyclic depsipeptides having the following formula (I) by intramolecular cyclization.

  通过分子内环化制备具有以下式(I)的环状脱氨肽的方法。
• Design, synthesis and biological evaluation of dipeptides as novel non-covalent 20S proteasome inhibitors
  作者：Ya-Jun Yang、Ke Wang、Ying Yang、Fang-Fang Lai、Xiao-Guang Chen、Zhi-Yan Xiao

  DOI：10.1080/10286020.2021.1910241

  日期：2021.5.4
• A Latent Oxazoline Electrophile for N−O−C Bond Formation in Pseudomonine Biosynthesis
  作者：Elizabeth S. Sattely、Christopher T. Walsh

  DOI：10.1021/ja804499r

  日期：2008.9.17

  Nitrogen-heteroatom bonds figure prominently in the structural, chemical, and functional diversity of natural products. In the case of Pseudomonas siderophore pseudomonine, an N-O hydroxamate linkage is found uncommonly configured in an isoxazolidinone ring. In an effort to understand the biogenesis of this heterocycle, we have characterized the pseudomonine synthetase in vitro and reconstituted the complete biosynthetic pathway. Our results indicate that the isoxazolidinone of pseudomonine arises from spontaneous rearrangement of an oxazoline precursor. To the best of our knowledge, this is a previously uncharacterized mode of post-assembly line heterocyclization. Our results establish the oxygen of the ubiquitous siderophore hydroxamate functionality as a nucleophile and may be indicative of general strategy for N-O-C bond formation in nature.
• Discovery of novel non-covalent inhibitors selective to the β5-subunit of the human 20S proteasome
  作者：Kai Xu、Ke Wang、Ying Yang、Ding-An Yan、Li Huang、Chin-Ho Chen、Zhiyan Xiao

  DOI：10.1016/j.ejmech.2015.05.023

  日期：2015.6

  A series of linear peptides (6a-6o) were designed based on the known non-covalent 20S proteasome inhibitors TMC-95A and compound 5 via a fragment-based approach. These compounds were synthesized and evaluated against the chymotrypsin-like activity of the human 20S proteasome. Three of them (6d, 6e and 6k) were potent inhibitors with IC50 values at the submicromolar level. These three compounds were selective to the beta 5-subunit and showed no obvious inhibition against trypsin-like and caspase-like activities of the human 20S proteasome. Docking study of the most potent compound 6e revealed its key interactions with the beta 5-subunit of the 20S proteasome. These findings have provided a new chemical template for non-covalent proteasome inhibitors, which is ready for further structural optimization to improve both potency and subunit selectivity. (C) 2015 Elsevier Masson SAS. All rights reserved.