Fmoc-(R)-3-amino-2-methylpropan-1-ol | 1265892-29-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: Fmoc-(R)-3-amino-2-methylpropan-1-ol
• 英文别名: (9H-Fluoren-9-yl)methyl (R)-(3-hydroxy-2-methylpropyl)carbamate；9H-fluoren-9-ylmethyl N-[(2R)-3-hydroxy-2-methylpropyl]carbamate
• CAS: 1265892-29-2
• 化学式: C₁₉H₂₁NO₃
• 分子量: 311.381
• InChiKey: YWNRRDUADLHCJI-CYBMUJFWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.2
• 重原子数：
  23
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  58.6
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  Fmoc-(R)-3-amino-2-methylpropan-1-ol 在 Jones reagent 作用下， 以 丙酮 、 异丙醇 为溶剂， 反应 3.0h， 以233 mg的产率得到(R)-3-(Fmoc-氨基)-2-甲基丙酸
  参考文献：
  名称：

  Design Strategies for the Sequence-Based Mimicry of Side-Chain Display in Protein β-Sheets by α/β-Peptides

  摘要：

  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.

  DOI：

  10.1021/ja306311r
• 作为产物：
  描述：

  9-芴甲基-N-琥珀酰亚胺基碳酸酯 、 (R)-3-amino-2-methyl-1-propanol 在 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 为溶剂， 以367 mg的产率得到Fmoc-(R)-3-amino-2-methylpropan-1-ol
  参考文献：
  名称：

  Design Strategies for the Sequence-Based Mimicry of Side-Chain Display in Protein β-Sheets by α/β-Peptides

  摘要：

  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.

  DOI：

  10.1021/ja306311r

文献信息

• 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.