(S)-3-[(S)-3-((S)-3-tert-Butoxycarbonylamino-2,2,4-trimethyl-pentanoylamino)-2,2-dimethyl-butyrylamino]-2,2,5-trimethyl-hexanoic acid methyl ester | 499242-83-0

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: (S)-3-[(S)-3-((S)-3-tert-Butoxycarbonylamino-2,2,4-trimethyl-pentanoylamino)-2,2-dimethyl-butyrylamino]-2,2,5-trimethyl-hexanoic acid methyl ester
• CAS: 499242-83-0
• 化学式: C₂₉H₅₅N₃O₆
• 分子量: 541.772
• InChiKey: GEBGZDFOHWYUIS-ACRUOGEOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.82
• 重原子数：
  38.0
• 可旋转键数：
  12.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.86
• 拓扑面积：
  122.83
• 氢给体数：
  3.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  (S)-3-[(S)-3-((S)-3-tert-Butoxycarbonylamino-2,2,4-trimethyl-pentanoylamino)-2,2-dimethyl-butyrylamino]-2,2,5-trimethyl-hexanoic acid methyl ester 在 sodium hydroxide 、 N,N-二异丙基乙胺 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 氯仿 、 2,2,2-三氟乙醇 为溶剂， 反应 84.0h， 生成 methyl (3S)-3-[[(3S)-3-[[(3S)-3-[[(3S)-3-[[(3S)-2,2-dimethyl-3-[[(3S)-2,2,4-trimethyl-3-[(2-methylpropan-2-yl)oxycarbonylamino]pentanoyl]amino]butanoyl]amino]-2,2,5-trimethylhexanoyl]amino]-2,2,4-trimethylpentanoyl]amino]-2,2-dimethylbutanoyl]amino]-2,2,5-trimethylhexanoate
  参考文献：
  名称：

  摘要：

  The preparation of (S)-beta(2.2.3) -amino acids with two Me groups in the a-position and the side chains of Ala, Val, and Len in the P-position (double methylation of Boc-beta-HAla-OMe, Boc-beta-Val-OMe, and Boc-beta-LeuOMe, Scheme 2) is described. These beta-amino acids and unlabelled as well as specifically C-13- and (15)labelled 2,2-dimethyl-3-amino acid (beta(2.2)-HAib) derivatives have been coupled in solution (Schemes 1, 3 and 4) to give protected (N-Boc, C-OMe), partially protected (N-Boc/C-OH, N-H/C-OMe), and unprotected beta(2.2) - and beta(2.2.3)- hexapeptides, and beta(2.2) and beta(2.2.3)-heptapeptides 1-7. NMR Analyses in solution (Tables 1 and 2, and Figs. 2-4) and in the solid state (2D-MAS NMR measurements of the fully labelled BOC-(beta(2.2)-HAib)(6)-OMe ([C-13(30), N-15(6)]-1e; Fig. 5), and TEDOR/REDOR NMR investigations of mixtures (Fig. 6) of the unlabelled AC-([beta(2.2)-HAib)(7)- OMe (4) and of a labelled derivative ([C-13(4),N-15(2)]-5; Figs. 7- 11, and 19), a molecular-modeling study (Figs. 13 15), and a search in the Cambridge Crystallographic Data Base (Fig. 16) allow the following conclusions: i) there is no evidence for folding (helix or turn) or for aggregation to sheets of the geminally dimethyl substituted peptide chains in solution; ii) there are distinct conformational preferences of the individual beta(2.2) and beta(2.2.3)-amino acid residues: close to eclipsing around the C(O) - C(Me-2(CHR)) bond (tau(1.2)), almost perfect staggering around the C(2)-C(3) ethane bond (tau(2,3)), and antiperiplanar arrangement of H(C3) and H(N) (TIN; Fig. 12) in the solid state; iii) the beta(2,2)-peptides may be part of a turn structure with a ten-membered H-bonded ring; iv) the main structure present in the solid state of F3CCO(beta(2,2) -HAib)(7)-OMe is a nonfolded chain (>30 Angstrom between the termini and >20 Angstrom between the N-terminus and the CH2 group of residue 5) with all C = O bonds in a parallel alignment (+/-10degrees). With these structural parameters, a simple modelling was performed producing three (maybe four) possible chain geometries: one fully extended, two with parallel peptide planes (with zick-zack and crankshaft-type arrangement of the peptide bonds). and (possibly) a fourth with meander-like winding (D-G in Figs. 17 and 18).

  DOI：

  10.1002/1522-2675(200209)85:9<2877::aid-hlca2877>3.0.co;2-w
• 作为产物：
  描述：

  Pentanoic acid,3-[[(1,1-dimethylethoxy)carbonyl]amino]-2,2,4-trimethyl-, methyl ester,(3S)- 在 sodium hydroxide 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三乙胺 、 N,N-二异丙基乙胺 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 氯仿 、 2,2,2-三氟乙醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 109.0h， 生成 (S)-3-[(S)-3-((S)-3-tert-Butoxycarbonylamino-2,2,4-trimethyl-pentanoylamino)-2,2-dimethyl-butyrylamino]-2,2,5-trimethyl-hexanoic acid methyl ester
  参考文献：
  名称：

  摘要：

  The preparation of (S)-beta(2.2.3) -amino acids with two Me groups in the a-position and the side chains of Ala, Val, and Len in the P-position (double methylation of Boc-beta-HAla-OMe, Boc-beta-Val-OMe, and Boc-beta-LeuOMe, Scheme 2) is described. These beta-amino acids and unlabelled as well as specifically C-13- and (15)labelled 2,2-dimethyl-3-amino acid (beta(2.2)-HAib) derivatives have been coupled in solution (Schemes 1, 3 and 4) to give protected (N-Boc, C-OMe), partially protected (N-Boc/C-OH, N-H/C-OMe), and unprotected beta(2.2) - and beta(2.2.3)- hexapeptides, and beta(2.2) and beta(2.2.3)-heptapeptides 1-7. NMR Analyses in solution (Tables 1 and 2, and Figs. 2-4) and in the solid state (2D-MAS NMR measurements of the fully labelled BOC-(beta(2.2)-HAib)(6)-OMe ([C-13(30), N-15(6)]-1e; Fig. 5), and TEDOR/REDOR NMR investigations of mixtures (Fig. 6) of the unlabelled AC-([beta(2.2)-HAib)(7)- OMe (4) and of a labelled derivative ([C-13(4),N-15(2)]-5; Figs. 7- 11, and 19), a molecular-modeling study (Figs. 13 15), and a search in the Cambridge Crystallographic Data Base (Fig. 16) allow the following conclusions: i) there is no evidence for folding (helix or turn) or for aggregation to sheets of the geminally dimethyl substituted peptide chains in solution; ii) there are distinct conformational preferences of the individual beta(2.2) and beta(2.2.3)-amino acid residues: close to eclipsing around the C(O) - C(Me-2(CHR)) bond (tau(1.2)), almost perfect staggering around the C(2)-C(3) ethane bond (tau(2,3)), and antiperiplanar arrangement of H(C3) and H(N) (TIN; Fig. 12) in the solid state; iii) the beta(2,2)-peptides may be part of a turn structure with a ten-membered H-bonded ring; iv) the main structure present in the solid state of F3CCO(beta(2,2) -HAib)(7)-OMe is a nonfolded chain (>30 Angstrom between the termini and >20 Angstrom between the N-terminus and the CH2 group of residue 5) with all C = O bonds in a parallel alignment (+/-10degrees). With these structural parameters, a simple modelling was performed producing three (maybe four) possible chain geometries: one fully extended, two with parallel peptide planes (with zick-zack and crankshaft-type arrangement of the peptide bonds). and (possibly) a fourth with meander-like winding (D-G in Figs. 17 and 18).

  DOI：

  10.1002/1522-2675(200209)85:9<2877::aid-hlca2877>3.0.co;2-w