(3S)-3-[(3aR,5R,6S,6aR)-6-methoxy-2,2-dimethyl-3a,5,6,6a-tetrahydrofuro[2,3-d][1,3]dioxol-5-yl]-3-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid | 758711-28-3

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: (3S)-3-[(3aR,5R,6S,6aR)-6-methoxy-2,2-dimethyl-3a,5,6,6a-tetrahydrofuro[2,3-d][1,3]dioxol-5-yl]-3-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid
• CAS: 758711-28-3
• 化学式: C₁₆H₂₇NO₈
• 分子量: 361.392
• InChiKey: RIGHMYWTYDXCMQ-JUJYEKSXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.5
• 重原子数：
  25
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  113
• 氢给体数：
  2
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  (3S)-3-[(3aR,5R,6S,6aR)-6-methoxy-2,2-dimethyl-3a,5,6,6a-tetrahydrofuro[2,3-d][1,3]dioxol-5-yl]-3-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid 在 silver benzoate 、 氯甲酸乙酯 、 三乙胺 作用下， 以 四氢呋喃 为溶剂， 反应 0.5h， 生成 (S)-4-tert-Butoxycarbonylamino-4-((3aR,5R,6S,6aR)-6-methoxy-2,2-dimethyl-tetrahydro-furo[2,3-d][1,3]dioxol-5-yl)-butyric acid methyl ester
  参考文献：
  名称：

  γ-肽中的左撇子9螺旋：寡聚体的合成和构象研究，该寡聚体具有C-连接的car-gamma4-氨基酸和γ-氨基丁酸的二肽重复序列。

  摘要：

  DOI：

  10.1002/anie.200504380
• 作为产物：
  描述：

  methyl (3S)-3-[(tert-butoxy)carbonylamino]-3-[6-methoxy-2,2-dimethyl-(3aR,6S,6aR)-tetrahydrofuro-[2,3-d][1,3]dioxol-5-yl]propanoate 在 水 、 sodium hydroxide 作用下， 以 甲醇 为溶剂， 以85%的产率得到(3S)-3-[(3aR,5R,6S,6aR)-6-methoxy-2,2-dimethyl-3a,5,6,6a-tetrahydrofuro[2,3-d][1,3]dioxol-5-yl]-3-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid
  参考文献：
  名称：

  α/β-肽的设计：三残基转角基序和非手性甘氨酸对螺旋和转角的影响的研究

  摘要：

  新颖的三残基螺旋-转角二级结构，在N末端由一个螺旋形核，在肽生成具有“β-Caa-大号-Ala-大号-Ala，”“β-Caa-大号-Ala-γ- Caa'和'β-Caa- L -Ala -δ-Caa'（其中β - Caa是C-连接的碳-β-氨基酸，γ - Caa是C-连接的碳-γ-氨基酸，而δ -Caa是C末端的C-连接的碳δ-氨基酸）。这些转弯结构通过NH（i）/ CO（i +2）（i +2是肽中的最后一个残基）之间的12元，14元和15元（mr）氢键来稳定（i +2是肽中的最后一个残基） CO（i）/ NH（i）之间的mr氢键+2）。此外，设计了一系列α/β-肽，并用交替的甘氨酸（Gly）和（S）-β-Caa合成，以研究非手性α残基对螺旋结构和螺旋结构的影响。与以前的结果相反，C末端的三个“β-α-β”残基（α-残基为Gly）仅通过13-mr的正向氢键（类似于一个α-转角）来稳定。进行

  DOI：

  10.1002/asia.201000438

文献信息

• Hybrid Helices: Motifs for Secondary Structure Scaffolds in Foldamers
  作者：Gangavaram V. M. Sharma、Nagula Chandramouli、Madavi Choudhary、Pendem Nagendar、Kallaganti V. S. Ramakrishna、Ajit C. Kunwar、Peter Schramm、Hans-Jörg Hofmann

  DOI：10.1021/ja907074u

  日期：2009.12.2

  The concept of "hybrid helices" as a new motif for foldamers is presented. Hybrid helices can be realized by a combination of two or more different types of homologous and hybrid peptides, for example, beta-peptides and alpha/beta- and alpha/gamma-hybrid peptides, within the same oligomer. The different helix types of the various peptide foldamer classes are maintained and form a regular helix along the sequence of the oligomer. The transition from one helix type to another was found to be rather smooth with high compatibility of the different helix types. Such hybrid helices represent novel motifs of secondary structure scaffolds. They open up the possibility to change the direction of helix propagation in a subtle manner. Hybrid helices enrich the arsenal of defined foldamer structures for a structural and functional mimicry of native peptides and proteins.
• Robust Mixed 10/12 Helices Promoted by “Alternating Chirality” in a New Family of C-Linked Carbo-β-peptides
  作者：Gangavaram V. M. Sharma、K. Ravinder Reddy、Palakodety Radha Krishna、A. Ravi Sankar、K. Narsimulu、S. Kiran Kumar、P. Jayaprakash、B. Jagannadh、A. C. Kunwar

  DOI：10.1021/ja035752i

  日期：2003.11.1

  The C-linked carbo-beta-peptides, oligomers of a new class of C-linked carbo-beta3-amino acids, have been shown to generate mixed 12/10 and 10/12 helices. The design involves use of "alternating chirality" of the epimeric (at the amine center) monomers to control the stability of these helices. The observation of stable 12/10 helix in a tripeptide and 10/12 helix in a tetrapeptide is unprecedented.
• Self-Assembling Cyclic Tetrapeptide from Alternating C-Linked Carbo-β-amino Acid [(<i>S</i>)-β-Caa] and α-Aminoxy Acid [(<i>R</i>)-Ama]: A Selective Chloride Ion Receptor
  作者：Gangavaram V. M. Sharma、Vennampalli Manohar、Samit Kumar Dutta、Bojja Sridhar、Venna Ramesh、Ragampeta Srinivas、Ajit C. Kunwar

  DOI：10.1021/jo901923q

  日期：2010.2.19

  A cyclic tetrapeptide is prepared from alternating (S)-beta-Caa (C-linked carbo-beta-amino acid) and (R)-Ama (alpha-aminoxy acid). Extensive NMR (in CDCl(3) solution) and mass spectral (MS) studies show its halide binding capacity, with a special affinity to the chloride ion. At higher concentration it was found to form molecular aggregates its evidenced from transmission electron microscopic and atomic force microscopic analysis, confirming the formation of nanorods.
• The Design of α/β-Peptides: Study on Three-Residue Turn Motifs and the Influence of Achiral Glycine on Helix and Turn
  作者：Gangavaram V. M. Sharma、Nagula Chandramouli、Shaik Jeelani Basha、Pendem Nagendar、Kallaganti V. S. Ramakrishna、Akella V. S. Sarma

  DOI：10.1002/asia.201000438

  日期：2011.1.3

  Novel three‐residue helix‐turn secondary structures, nucleated by a helix at the N terminus, were generated in peptides that have ‘β‐Caa‐L‐Ala‐L‐Ala,’ ‘β‐Caa‐L‐Ala‐γ‐Caa,’ and ‘β‐Caa‐L‐Ala‐δ‐Caa’ (in which β‐Caa is C‐linked carbo‐β‐amino acid, γ‐Caa is C‐linked carbo‐γ‐amino acid, and δ‐Caa is C‐linked carbo‐δ‐amino acid) at the C terminus. These turn structures are stabilized by 12‐, 14‐, and 15‐membered

  新颖的三残基螺旋-转角二级结构，在N末端由一个螺旋形核，在肽生成具有“β-Caa-大号-Ala-大号-Ala，”“β-Caa-大号-Ala-γ- Caa'和'β-Caa- L -Ala -δ-Caa'（其中β - Caa是C-连接的碳-β-氨基酸，γ - Caa是C-连接的碳-γ-氨基酸，而δ -Caa是C末端的C-连接的碳δ-氨基酸）。这些转弯结构通过NH（i）/ CO（i +2）（i +2是肽中的最后一个残基）之间的12元，14元和15元（mr）氢键来稳定（i +2是肽中的最后一个残基） CO（i）/ NH（i）之间的mr氢键+2）。此外，设计了一系列α/β-肽，并用交替的甘氨酸（Gly）和（S）-β-Caa合成，以研究非手性α残基对螺旋结构和螺旋结构的影响。与以前的结果相反，C末端的三个“β-α-β”残基（α-残基为Gly）仅通过13-mr的正向氢键（类似于一个α-转角）来稳定。进行
• A Left-Handed 9-Helix in γ-Peptides: Synthesis and Conformational Studies of Oligomers with Dipeptide Repeats of C-Linked Carbo-γ4-amino Acids and γ-Aminobutyric Acid
  作者：Gangavaram V. M. Sharma、Pagadala Jayaprakash、Kongari Narsimulu、Ampapathi Ravi Sankar、Kondreddy Ravinder Reddy、Palakodety Radha Krishna、Ajit C. Kunwar

  DOI：10.1002/anie.200504380

  日期：2006.4.28