Ac-L-Phe-L-Arg-NH2 | 110392-41-1

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: Ac-L-Phe-L-Arg-NH2
• 英文别名: Ac-Phe-Arg-NH2；(2S)-2-[[(2S)-2-acetamido-3-phenylpropanoyl]amino]-5-(diaminomethylideneamino)pentanamide
• CAS: 110392-41-1
• 化学式: C₁₇H₂₆N₆O₃
• 分子量: 362.432
• InChiKey: KFDMLJZPFWESES-KBPBESRZSA-N

物化性质

• 密度：
  1.32±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.1
• 重原子数：
  26
• 可旋转键数：
  10
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.41
• 拓扑面积：
  166
• 氢给体数：
  5
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  N-Fmoc-N'-Boc-L-鸟氨酸 在 N-甲基吗啉 、 三乙胺 、 三氟乙酸 、 氯甲酸异丁酯 作用下， 以 四氢呋喃 、 乙二醇二甲醚 、 二氯甲烷 为溶剂， 反应 1.55h， 生成 Ac-L-Phe-L-Arg-NH2
  参考文献：
  名称：

  固链合成含精氨酸的肽和荧光基质的侧链锚定方法

  摘要：

  为了利用可用于多种修饰的α-羧基，包括掺入荧光团以制备荧光底物，有时需要通过其侧链将氨基酸连接到固相支持物上。与大多数其他氨基酸相反，将精氨酸的胍基锚定在树脂上需要使用辅助连接子。为了避免此类接头通常的多步合成及其与胍基的困难连接，我们开发了一种简单的方法，其中胍基是基于Rink酰胺树脂构建的。我们的策略遵循形成胍的步骤：（i）将鸟氨酸的异硫氰酸酯衍生物加到固体载体的氨基上，得到Nω-连接的硫代瓜氨酸；（ii）S-硫脲的甲基化；（iii）使用乙酸铵的胍基化。树脂的裂解产生了含精氨酸的化合物，树脂的胺基成为胍的一部分。我们已经通过合成一系列胰蛋白酶样丝氨酸蛋白酶的荧光底物证明了该方法的有效性，这些底物以高产率和高纯度获得。然后，我们的策略还允许从相同的前体差异取代的精氨酸衍生物（包括Nω-甲基和Nω-乙基精氨酸）生成。与中间体硫代瓜氨酸和S一起制备此类类似物的能力独特的前体生成的-甲基异硫代

  DOI：

  10.1021/jo048792t

文献信息

• .alpha.-Melanotropin: the minimal active sequence in the frog skin bioassay
  作者：Victor J. Hruby、Brian C. Wilkes、Mac E. Hadley、Fahad Al-Obeidi、Tomi K. Sawyer、Douglas J. Staples、Ann E. DeVaux、Orin Dym、Ana Maria de L. Castrucci

  DOI：10.1021/jm00394a033

  日期：1987.11

  yielded the peptide, Ac-alpha-MSH4-12-NH2 with a 360-fold increase in potency relative to Ac-alpha-MSH4-10-NH2. This peptide was only about 6-fold less potent than alpha-MSH. A series of Nle-4-substituted analogues also were prepared. Ac-[Nle4]-alpha-MSH4-10-NH2 was about 4 times more potent than Ac-alpha-MSH4-10-NH2. Ac-[Nle4]-alpha-MSH4-11-NH2 also was about 4 times more potent than Ac-alpha-MSH4-10-NH2

  在青蛙（Rpi pipiens）皮肤生物测定中确定了α-MSH（α-促黑素，α-黑素细胞刺激激素）的生物学活性所需的最小序列。引发可测量的生物学活性所需的序列是中央四肽序列Ac-His-Phe-Arg-Trp-NH2（Ac-alpha-MSH6-9-NH2），其效力比天然三肽低约6个数量级。 。此序列的较小片段（Ac-His-Phe-NH2，Ac-Phe-Arg-NH2，Ac-His-Phe-Arg-NH2）在高达10（-4）M的浓度下均不具有黑色素活性。无法证明四肽Ac-Phe-Arg-Trp-Gly-NH2（Ac-alpha-MSH7-10-NH2）和包括Ac-Lys-Pro-Val-NH2（ Ac-alpha-MSH11-13-NH2）。我们准备了一系列α-MSH的片段类似物，以试图确定每个氨基酸对天然激素的生物学活性的贡献。通过在C末端添加甘氨酸，可将Ac-alpha-MSH6-9
• Mapping the binding site of tissue kallikrein: preparation and testing of all possible substrate analog inhibitors homologous with the sequence of kininogen between Ser386 and Gln392
  作者：Milind S. Deshpande、James Burton

  DOI：10.1021/jm00095a002

  日期：1992.8

  Programs aimed at converting peptide inhibitors of proteolytic enzymes into more traditional drug structures require an understanding of the role played by the individual amino acid residues in the inhibitor. To this end, all possible substrate analogues occurring within the sequence Ser-Pro-Phe-Arg-Ser-Val-Gln392 from bovine kininogen were synthesized and tested as inhibitors of tissue kallikrein (EC 3.4.21.35, beta-PPK). Of the 21 sequences which can be formed from the heptapeptide, 11 have inhibitory constants which could be measured in the chromogenic assay employed in these studies. No dipeptide and only one tripeptide, Ac-Phe-Arg-Ser-NH2 (K(i) = 718-mu-M), measurably inhibits the enzyme. All longer peptides inhibit beta-PPK. The heptapeptide Ac-Ser-Pro-Phe-Arg-Ser-Val-Gln-NH2 is the most effective inhibitor in this series (K(i) = 101-mu-M). Each amino acid residue in the sequence appears to alter binding in a relatively independent manner. The N-terminal seryl residue (P4) and the prolyl residue (P3) slightly improve the K(i) of the various inhibitors. The phenylalanyl residue at P2 appears to have a more pronounced effect on K(i). The arginyl residue at P1 and the seryl residue at P1' appear to be the most important residues in the inhibitory sequence. They contribute approximately one-third and one-fourth of the binding energy to the interaction between the substrate analogues and beta-PPK, respectively. The valyl residue at P2', and the C-terminal glutaminyl residue improve K(i) of each of the peptides tested. Almost 80% of the binding energy of the substrate analogue inhibitors comes from the core sequence Phe-Arg-Ser which occurs between P2 and P1'. Molecular models developed from the Chen-Bode coordinates of the aprotinin-beta-PPK complex have been used to interpret the results of these studies.
• HRUBY, VICTOR J.;WILKES, BRIAN C.;HADLEY, MAC E.;AL-OBEIDI, FAHAD;SAWYER,+, J. MED. CHEM., 30,(1987) N 11, 2126-2130
  作者：HRUBY, VICTOR J.、WILKES, BRIAN C.、HADLEY, MAC E.、AL-OBEIDI, FAHAD、SAWYER,+

  DOI：——

  日期：——