(2R,3S)-3-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-2-methylbutanoic acid | 266318-76-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: (2R,3S)-3-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-2-methylbutanoic acid
• 英文别名: (2R,3S)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-2-methylbutyric acid；Fmoc-(2R,3S)-β^2,3-HAla(α-Me)-OH；Fmoc-(2R,3S)-3-amino-2-methylbutanoic acid；(2R,3S)-3-(9H-fluoren-9-ylmethoxycarbonylamino)-2-methylbutanoic acid
• CAS: 266318-76-7
• 化学式: C₂₀H₂₁NO₄
• 分子量: 339.391
• InChiKey: XUIBECOXWZXNSY-OLZOCXBDSA-N

物化性质

• 沸点：
  556.1±33.0 °C(Predicted)
• 密度：
  1.229±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.6
• 重原子数：
  25
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.3
• 拓扑面积：
  75.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  NΒ-芴甲氧羰基-NΩ-叔丁氧羰基-L-Β-高赖氨酸 、 (2R,3S)-3-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-2-methylbutanoic acid 、 (2R,3S)-3-{[(9-H-fluoren-9-ylmethoxy)carbonyl]amino}-2,4-dimethylpentanoic acid 、 (2R,3S)-3-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-2,5-dimethylhexanoic acid 以90%的产率得到H-(2R,3S)-β^2,3-HAla(α-Me)-(2R,3S)-β²-HVal(α-Me)-(S)-β^2,3-HVal-(S)-β³-HLys-(2R,3S)-β^2,3-HAla-(2R,3S)-β^2,3-HLeu(α-Me)-OH*TFA
  参考文献：
  名称：

  Structure and Conformation ofβ-Oligopeptide Derivatives with Simple Proteinogenic Side Chains: Circular Dichroism and Molecular Dynamics Investigations

  摘要：

  DOI：

  10.1002/(sici)1522-2675(20000119)83:1<34::aid-hlca34>3.0.co;2-b
• 作为产物：
  描述：

  tert-butyl (2R,3S,αS)-3-[benzyl(α-methylbenzyl)amino]-2-methylbutanoate 在 palladium dihydroxide 氢气 、 sodium carbonate 作用下， 以 乙酸乙酯 、 丙酮 、 三氟乙酸 为溶剂， 反应 50.0h， 生成 (2R,3S)-3-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-2-methylbutanoic acid
  参考文献：
  名称：

  Structure and Conformation ofβ-Oligopeptide Derivatives with Simple Proteinogenic Side Chains: Circular Dichroism and Molecular Dynamics Investigations

  摘要：

  DOI：

  10.1002/(sici)1522-2675(20000119)83:1<34::aid-hlca34>3.0.co;2-b

文献信息

• NMR-Solution Structures of Fluoro-Substitutedβ-Peptides: A314-Helix and a Hairpin Turn. The First Case of a 90° OCCF Dihedral Angle in anα-Fluoro-Amide Group
  作者：Raveendra I. Mathad、Bernhard Jaun、Oliver Flögel、James Gardiner、Markus Löweneck、Jeroen D. C. Codée、Peter H. Seeberger、Dieter Seebach、Michael K. Edmonds、Florian H. M. Graichen、Andrew D. Abell

  DOI：10.1002/hlca.200790235

  日期：2007.12

  314-helical structure by enforcing the FCCO ap-conformation, we could now demonstrate that the same procedure leads to a structure with the unfavorable ca. 90° FCCO dihedral angle, enforced by the 314-helical folding in a β-tridecapeptide (cf.1; Fig. 4). This is interpreted as a consequence of cooperative folding in the longer β-peptide. A F-substituent placed in the turn section of a β-peptidic hairpin turn

  为了进一步研究的偏好antiperiplanar（AP）构象α氟酰胺基，二β -肽，1和2，含有（2-F） - β 3哈拉和（2-F） - β 2已合成了hPhe残基。确定了它们在CD 3 OH中的NMR溶液结构，并与非F取代的类似物3和4a进行了比较。虽然我们在之前的调查发现（阖闾化学学报2005，88，266），该一个立体有择引入F-取代基在一个的中心位置β -庚肽能够“破”的3 14通过强制执行FCCO螺旋结构AP -conformation，我们现在可以证明，相同的过程导致具有不利ca的结构。90°FCCO二面角，强迫由3 14在螺旋折叠β -十三碳肽（参见1 ;图4）。这被解释为在较长的β-肽中协同折叠的结果。F取代基放置在β -peptidic发夹转角被证明是在AP -arrangement相对于相邻的CO键（参见2 ;图7）。分析非-F-取代β -tetrapeptides（与两个中央的螺旋防止配置β
• Design Strategies for the Sequence-Based Mimicry of Side-Chain Display in Protein β-Sheets by α/β-Peptides
  作者：George A. Lengyel、W. Seth Horne

  DOI：10.1021/ja306311r

  日期：2012.9.26

  The sophistication of folding patterns and functions displayed by unnatural-backbone oligomers has increased tremendously in recent years. Design strategies for the mimicry of tertiary structures seem within reach; however, a general method for the mimicry of sheet segments in the context of a folded protein is an unmet need preventing realization of this goal. Previous work has shown that 1 -> 1 alpha ->beta-residue substitutions at cross-strand positions in a hairpin-forming alpha-peptide sequence can generate an alpha/beta-peptide analogue that folds in aqueous conditions but with a change in side-chain display relative to the natural sequence; this change would prevent application of single beta-residue substitutions in a larger protein. Here, we evaluate four different substitution strategies based on replacement of alpha alpha dipeptide segments for the ability to retain both sheet folding encoded by a parent alpha-peptide sequence as well as nativelike side-chain display in the vicinity of the beta-residue insertion point. High-resolution structure determination and thermodynamic analysis of folding by multidimensional NMR suggest that three of the four designs examined are applicable to larger proteins.