(S)-7-(2-Chloro-benzyloxycarbonylamino)-3-{(S)-2-[(9H-fluoren-9-ylmethoxycarbonylamino)-methyl]-3-methyl-butyrylamino}-heptanoic acid benzyl ester | 888966-29-8

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: (S)-7-(2-Chloro-benzyloxycarbonylamino)-3-{(S)-2-[(9H-fluoren-9-ylmethoxycarbonylamino)-methyl]-3-methyl-butyrylamino}-heptanoic acid benzyl ester
• CAS: 888966-29-8
• 化学式: C₄₃H₄₈ClN₃O₇
• 分子量: 754.323
• InChiKey: QYHBUEVOGRDBJY-NBWQQBAWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.17
• 重原子数：
  54.0
• 可旋转键数：
  18.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  132.06
• 氢给体数：
  3.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  (S)-7-(2-Chloro-benzyloxycarbonylamino)-3-{(S)-2-[(9H-fluoren-9-ylmethoxycarbonylamino)-methyl]-3-methyl-butyrylamino}-heptanoic acid benzyl ester 在 palladium on activated charcoal 氢气 、 溶剂黄146 作用下， 以 乙醇 、 二氯甲烷 为溶剂， 反应 26.0h， 生成 H-(S)-β³hHis-(2R,3S)-β^2,3hAla(αMe)-(2R,3S)-β^2,3hAla(αMe)-(S)-β²hVal-(S)-β³hLys-(2R,3S)-β^2,3hAla(αMe)-(2R,3S)-β^2,3hAla(αMe)-(R)-β³hCys-OH
  参考文献：
  名称：

  β-肽二级结构通过 Zn2+ 络合强化和强化——在通往β-肽锌指的道路上？

  摘要：

  The correlation between beta(2)-, beta(3)-, and beta(2,3)-amino acid-residue configuration and stability of helix and hairpin-turn secondary structures of peptides consisting of homologated proteinogenic amino acids is analyzed (Figs. 1-3). To test the power of Zn2+ ions in fortifying and/or enforcing secondary structures of beta-peptides, a beta-decapeptide, 1, four beta-octapeptides, 2-5, and a P-hexadecapeptide, 10, have been devised and synthesized. The design was such that the peptides would a) fold to a 14-helix (I and 3) or a hairpin turn (2 and 4), or form neither of these two secondary structures (i.e., 5), and b) carry the side chains of cysteine and histidine in positions, which will allow Zn2+ ions to use their extraordinary affinity for RS- and the imidazole N-atoms for stabilizing or destabilizing the intrinsic secondary structures of the peptides. Tlie beta-hexadecapeptide 10 was designed to a) fold to a turn, to which a 14-helical structure is attached through a P-dipeptide spacer, and b) contain two cysteine and two histidine side chains for Zn complexation, in order to possibly mimic a Zn-finger motif While CD spectra (Figs6-8 and 17) and ESI mass spectra (Figs. 9 and 18) are compatible with the expected effects of Zn 21 ions in all cases, it was shown by detailed NMR analyses of three of the peptides, i.e., 2, 3,5, in the absence and presence of ZnCl2, that i) beta-peptide 2 forms a hairpin turn in H2O, even without Zn complexation to the terminal beta(3)hHis and 3 hCys side chains (Fig. 11), ii) beta-peptide 3, which is present as a 14-helix in MeOH, is forced to a hairpin-turn structure by Zn complexation in H2O (Fig. 12), and iii) beta-peptide 5 is poorly ordered in CD3OH (Fig. 13) and in H2O (Fig. 14), with far-remote beta(3)hCys and beta(3)hHis residues, and has a distorted turn structure in the presence of Zn 21 ions in H2O, with proximate terminal Cys and His side chains.

  DOI：

  10.1002/hlca.339
• 作为产物：
  描述：

  、 FMOC-(S)-2-(二甲基)-3-甲基丁酸 在 N-甲基吗啉 、 Methanaminium,N-[(dimethylamino)(3H-1,2,3-triazolo[4,5-b]pyridin-3-yloxy)methylene]-N-methyl-, hexafluorophosphate(1-) 作用下， 以 二氯甲烷 为溶剂， 生成 (S)-7-(2-Chloro-benzyloxycarbonylamino)-3-{(S)-2-[(9H-fluoren-9-ylmethoxycarbonylamino)-methyl]-3-methyl-butyrylamino}-heptanoic acid benzyl ester
  参考文献：
  名称：

  β-肽二级结构通过 Zn2+ 络合强化和强化——在通往β-肽锌指的道路上？

  摘要：

  The correlation between beta(2)-, beta(3)-, and beta(2,3)-amino acid-residue configuration and stability of helix and hairpin-turn secondary structures of peptides consisting of homologated proteinogenic amino acids is analyzed (Figs. 1-3). To test the power of Zn2+ ions in fortifying and/or enforcing secondary structures of beta-peptides, a beta-decapeptide, 1, four beta-octapeptides, 2-5, and a P-hexadecapeptide, 10, have been devised and synthesized. The design was such that the peptides would a) fold to a 14-helix (I and 3) or a hairpin turn (2 and 4), or form neither of these two secondary structures (i.e., 5), and b) carry the side chains of cysteine and histidine in positions, which will allow Zn2+ ions to use their extraordinary affinity for RS- and the imidazole N-atoms for stabilizing or destabilizing the intrinsic secondary structures of the peptides. Tlie beta-hexadecapeptide 10 was designed to a) fold to a turn, to which a 14-helical structure is attached through a P-dipeptide spacer, and b) contain two cysteine and two histidine side chains for Zn complexation, in order to possibly mimic a Zn-finger motif While CD spectra (Figs6-8 and 17) and ESI mass spectra (Figs. 9 and 18) are compatible with the expected effects of Zn 21 ions in all cases, it was shown by detailed NMR analyses of three of the peptides, i.e., 2, 3,5, in the absence and presence of ZnCl2, that i) beta-peptide 2 forms a hairpin turn in H2O, even without Zn complexation to the terminal beta(3)hHis and 3 hCys side chains (Fig. 11), ii) beta-peptide 3, which is present as a 14-helix in MeOH, is forced to a hairpin-turn structure by Zn complexation in H2O (Fig. 12), and iii) beta-peptide 5 is poorly ordered in CD3OH (Fig. 13) and in H2O (Fig. 14), with far-remote beta(3)hCys and beta(3)hHis residues, and has a distorted turn structure in the presence of Zn 21 ions in H2O, with proximate terminal Cys and His side chains.

  DOI：

  10.1002/hlca.339