Ac-RHYINLITRLRY-NH₂ | 1471195-56-8

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: Ac-RHYINLITRLRY-NH₂
• 英文别名: (2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-acetamido-5-(diaminomethylideneamino)pentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylpentanoyl]amino]-N-[(2S)-1-[[(2S,3S)-1-[[(2S,3R)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]butanediamide
• CAS: 1471195-56-8
• 化学式: C₇₆H₁₂₃N₂₅O₁₇
• 分子量: 1658.97
• InChiKey: LTZAFDDHKCKLIF-OQXRNXRFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1
• 重原子数：
  118
• 可旋转键数：
  56
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  710
• 氢给体数：
  27
• 氢受体数：
  21

反应信息

• 作为产物：
  描述：

  Fmoc-L-亮氨酸 、 乙酸酐 、 Fmoc-L-异亮氨酸 、 Fmoc-O-叔丁基-L-酪氨酸 、 Fmoc-O-叔丁基-L-苏氨酸 、 Fmoc-N-三苯甲基-L-天冬酰胺 、 N-Fmoc-N'-三苯甲基-L-组氨酸 、 alkaline earth salt of/the/ methylsulfuric acid 在 1-羟基苯并三唑 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 、 哌啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 Ac-RHYINLITRLRY-NH₂
  参考文献：
  名称：

  Replacement of Thr³² and Gln³⁴ in the C-Terminal Neuropeptide Y Fragment 25–36 by cis-Cyclobutane and cis-Cyclopentane β-Amino Acids Shifts Selectivity toward the Y₄ Receptor

  摘要：

  Neuropeptide Y (NPY) and pancreatic polypeptide (PP) control central and peripheral processes by activating the G protein coupled receptors YxR (x = 1, 2, 4, 5). We present analogs of the C-terminal fragments 25-36 and 32-36 of NPY and PP containing (1R,2S)-cyclobutane (beta Cbu) or (1R,2S)cyclopentane (beta 6Cpe) fl-amino acids, which display exclusively Y4R affinity. In particular, [beta Cpe(34)]-NPY-(25-36) is a Y4R selective partial agonist (EC50 41 +/- 6 nM, E-max 71%) that binds Y4R with a K-i of 10 +/- 2 nM and a selectivity >100-fold relative to YiR ancrY2R and >50-fold relative to Y5R Comparably, [Y-32, beta Cpe(34)-NPY(PP)-(32-36) selectively binds and activates Y4R (EC50 94 +/- 21 nM, E-max 73%). The NMR structure of [beta Cpe(34)]NPY-(25-36) in dodecylphosphatidylcholine micelles shows a short helix at residues 27-32, while the C-terminal segment R-33 beta Cpe(34)R(35)Y(36) is extended. The biological properties of the,beta Cbu- or beta Cpe-containing NPY and PP C-terminal fragments encourage the future application of these beta-amino acids in the synthesis of selective Y4R ligands.

  DOI：

  10.1021/jm4008505