(2S,5R)-2,5-dihydro-3,6-diethoxy-2-isopropyl-5-(4-bromobutyl)pyrazine | 185335-83-5

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 甲亚胺酸及其衍生物
• 英文名称: (2S,5R)-2,5-dihydro-3,6-diethoxy-2-isopropyl-5-(4-bromobutyl)pyrazine
• 英文别名: (2R,5S)-2-(4-bromobutyl)-3,6-diethoxy-5-propan-2-yl-2,5-dihydropyrazine
• CAS: 185335-83-5
• 化学式: C₁₅H₂₇BrN₂O₂
• 分子量: 347.296
• InChiKey: RKCJOQOMQIBFJK-OLZOCXBDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  20
• 可旋转键数：
  9
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.87
• 拓扑面积：
  43.2
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (2S,5R)-2,5-dihydro-3,6-diethoxy-2-isopropyl-5-(4-bromobutyl)pyrazine 在 盐酸 、 硫化氢 、 potassium tert-butylate 、 mercury(II) diacetate 、 三氟乙酸 作用下， 以 四氢呋喃 为溶剂， 生成 (R)-6-(Acetylamino-methylsulfanyl)-2-amino-hexanoic acid ethyl ester
  参考文献：
  名称：

  A General Method for Constraining Short Peptides to an α-Helical Conformation

  摘要：

  A method for constraining short peptides (<20 residues) of arbitrary sequence to an alpha-helical conformation (similar to 100% helical in H2O at 25 degrees C) is presented. Glutamine residues at positions i and i + 7 of the peptides were tethered with an alkanediyl chain between the side chain nitrogen atoms. Peptides containing this tether were readily synthesized on the solid phase by amide formation between an alpha,omega-diaminoallcane and the side chain carboxylates of glutamate residues. The resulting cyclic peptides were studied by NMR and CD and were found to adopt an alpha-helical conformation in aqueous solution. The alpha-helix was thermally stable to greater than or equal to 40 degrees C. Corresponding untethered control peptides with N-methylglutamine at the i and i + 7 positions lacked helicity under the same conditions. Analogous peptides were also prepared for comparison using the thiolysine cross-linking method described previously [Jackson, D. Y.; King, D. S.; Chmielewski, J.; Singh, S.; Schultz, P. G. J. Am Chem. Soc. 1991, 113, 9391-9392].

  DOI：

  10.1021/ja9611654
• 作为产物：
  描述：

  1,4-二溴丁烷 、 (S)-2,5-二氢-3,6-二乙氧基-2-异丙基吡嗪 在 正丁基锂 作用下， 以 四氢呋喃 、 乙酸乙酯 为溶剂， 以57%的产率得到(2S,5R)-2,5-dihydro-3,6-diethoxy-2-isopropyl-5-(4-bromobutyl)pyrazine
  参考文献：
  名称：

  Constrained helical peptides and methods of making same

  摘要：

  提供了具有约束区域的环肽，其具有α-螺旋构象。提供了具有来自HIV gp41的氨基酸序列的约束螺旋肽，并提供了它们在制备可预防病毒膜融合的抗体中的应用。还提供了制备这种环肽的方法。

  公开号：

  US06271198B1

文献信息

• CONSTRAINED HELICAL PEPTIDES AND METHODS OF MAKING SAME
  申请人：Genentech, Inc.

  公开号：EP0938497A1

  公开（公告）日：1999-09-01
• US6271198B1
  申请人：——

  公开号：US6271198B1

  公开（公告）日：2001-08-07
• [EN] CONSTRAINED HELICAL PEPTIDES AND METHODS OF MAKING SAME<br/>[FR] PEPTIDE A STRUCTURE HELICOIDALE CONTRAINTE ET LEURS PROCEDES DE FABRICATION
  申请人：GENENTECH, INC.

  公开号：WO1998020036A1

  公开（公告）日：1998-05-14

  (EN) Provided are cyclized peptides with a constrained region(s) having an $g(a)-helical conformation. Constrained helical peptides having amino acid sequences from HIV gp41 are provided, as is their use in preparing antibodies that prevent viral membrane fusion. Also provided are methods for making such cyclized peptides.(FR) L'invention porte sur des peptides cyclisés possédant une (des) région(s) contrainte(s) à structure hélicoïdale $g(a). L'invention porte également sur des peptides à structure hélicoïdale contrainte possédant des séquences d'acides aminés issues de la protéine gp41 du VIH, sur leur utilisation dans la préparation d'anticorps qui préviennent la fusion membranaire virale, ainsi que sur des procédés de fabrication de ces peptides cyclisés.
• Constrained helical peptides and methods of making same
  申请人：Genentech, Inc.

  公开号：US06271198B1

  公开（公告）日：2001-08-07

  Provided are cyclized peptides with a constrained region(s) having an &agr;-helical conformation. Constrained helical peptides having amino acid sequences from HIV gp41 are provided, as is their use in preparing antibodies that prevent viral membrane fusion. Also provided are methods for making such cyclized peptides.

  提供了具有约束区域的环肽，其具有α-螺旋构象。提供了具有来自HIV gp41的氨基酸序列的约束螺旋肽，并提供了它们在制备可预防病毒膜融合的抗体中的应用。还提供了制备这种环肽的方法。
• A General Method for Constraining Short Peptides to an α-Helical Conformation
  作者：J. Christopher Phelan、Nicholas J. Skelton、Andrew C. Braisted、Robert S. McDowell

  DOI：10.1021/ja9611654

  日期：1997.1.1

  A method for constraining short peptides (<20 residues) of arbitrary sequence to an alpha-helical conformation (similar to 100% helical in H2O at 25 degrees C) is presented. Glutamine residues at positions i and i + 7 of the peptides were tethered with an alkanediyl chain between the side chain nitrogen atoms. Peptides containing this tether were readily synthesized on the solid phase by amide formation between an alpha,omega-diaminoallcane and the side chain carboxylates of glutamate residues. The resulting cyclic peptides were studied by NMR and CD and were found to adopt an alpha-helical conformation in aqueous solution. The alpha-helix was thermally stable to greater than or equal to 40 degrees C. Corresponding untethered control peptides with N-methylglutamine at the i and i + 7 positions lacked helicity under the same conditions. Analogous peptides were also prepared for comparison using the thiolysine cross-linking method described previously [Jackson, D. Y.; King, D. S.; Chmielewski, J.; Singh, S.; Schultz, P. G. J. Am Chem. Soc. 1991, 113, 9391-9392].