Boc-Tyr(Br-Z)-OH | 75974-78-6

• 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: Boc-Tyr(Br-Z)-OH
• 英文别名: (2S)-3-[4-[(4-bromophenyl)methoxycarbonyloxy]phenyl]-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid
• CAS: 75974-78-6
• 化学式: C₂₂H₂₄BrNO₇
• 分子量: 494.339
• InChiKey: IIOZFXUDZZKIBV-SFHVURJKSA-N

物化性质

• 沸点：
  638.3±55.0 °C(Predicted)
• 密度：
  1.414±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.9
• 重原子数：
  31
• 可旋转键数：
  11
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  111
• 氢给体数：
  2
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  Boc-Tyr(Br-Z)-OH 在 palladium dihydroxide 氢气 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三氟乙酸 作用下， 以 甲醇 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 生成 methyl (2S)-2-[[(2S)-2-[[(2R,3S,4S,5R)-5-[[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]methyl]-3,4-dihydroxyoxolane-2-carbonyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoate
  参考文献：
  名称：

  Folded Conformation in Peptides Containing Furanoid Sugar Amino Acids

  摘要：

  DOI：

  10.1021/ja9816685

文献信息

• Synthesis of the Five Peptide Derivatives Needed to Build the Sequence Corresponding to 1–30 of Human Epidermal Growth Factor (h-EGF)
  作者：Song Yuh Shin、Yukihiko Kaburaki、Masanori Watanabe、Eisuke Munekata

  DOI：10.1271/bbb.56.399

  日期：1992.1

  For the classical solution synthesis of human epidermal growth factor (h-EGF), five protected peptide derivatives, Boc-Leu-Asp(OcHex)-Lys(Cl-Z)-Tyr(Br-Z)-Ala-OH (5), Boc-Val-Cys(MeBzl)-Met-Tyr(Br-Z)-Ile-Glu(OcHex)-Ala-OH (12), Boc-Tyr(Br-Z)-Cys(MeBzl)-Leu-His-Asp(OcHex)-Gly-OH (18), Boc-Cys(MeBzl)-Pro-Leu-Ser(Bzl)-His-Asp(OcHex)-Gly-O H (23) and Boc-Asn-Ser(Bzl)-Asp(OcHex)-Ser(Bzl)-Glu(OcHex)-OH (28) were synthesized to build up the sequence corresponding to 1–30.

  对于人表皮生长因子（h-EGF）的经典合成解决方案，合成了五种保护性肽衍生物，即Boc-Leu-Asp(OcHex)-Lys(Cl-Z)-Tyr(Br-Z)-Ala-OH（5），Boc-Val-Cys(MeBzl)-Met-Tyr(Br-Z)-Ile-Glu(OcHex)-Ala-OH（12），Boc-Tyr(Br-Z)-Cys(MeBzl)-Leu-His-Asp(OcHex)-Gly-OH（18），Boc-Cys(MeBzl)-Pro-Leu-Ser(Bzl)-His-Asp(OcHex)-Gly-O H（23）和Boc-Asn-Ser(Bzl)-Asp(OcHex)-Ser(Bzl)-Glu(OcHex)-OH（28），以构建对应于1-30的序列。
• Hydrolytic Cleavage of Pyroglutamyl-peptide Bond. V. Selective Removal of Pyroglutamic Acid from Biologically Active Pyroglutamylpeptides in High Concentrations of Aqueous Methanesulfonic Acid
  作者：Junko Kobayashi、Kazuhiro Ohki、Keiko Okimura、Tadashi Hashimoto、Naoki Sakura

  DOI：10.1248/cpb.54.827

  日期：——

  Application of aqueous methanesulfonic acid (MSA) for selective chemical removal of pyroglutamic acid (pGlu) residue from five biologically active pyroglutamyl-peptides (pGlu-X-peptides, X=amino acid residue at position 2) was examined. Gonadotropin releasing hormone (Gn-RH), dog neuromedin U-8 (d-NMU-8), physalaemin (PH), a bradykinin potentiating peptide (BPP-5a) and neurotensin (NT) as pGlu-X-peptides were incubated in either 70% or 90% aqueous MSA at 25 °C. HPLC analysis of the incubation solutions showed that the main decomposition product was H-X-peptide derived from each pGlu-X-peptide by the removal of pGlu. The results revealed that the pGlu-X peptide bond had higher susceptibility than various internal amide bonds in the five peptides examined, including the Trp-Ser bond in Gn-RH, the C-terminal Asn-NH2 in d-NMU-8, and the Asp-Pro bond in PH, whose acid susceptibility is well known. Thus, mild hydrolysis with high concentrations of aqueous MSA may be applicable to chemically selective removal of pGlu from pGlu-X-peptides for structural examinations.

  使用水溶性甲磺酸（MSA）选择性化学去除五种生物活性脯氨酸肽（pGlu-X-肽，X为位置2的氨基酸残基）中的脯氨酸残基的应用进行了研究。促性腺激素释放激素（Gn-RH）、犬神经肽U-8（d-NMU-8）、物理肽（PH）、一种缓激肽增效肽（BPP-5a）和神经肽（NT）作为pGlu-X肽，在25°C下分别在70%或90%的水溶性MSA中进行孵育。孵育溶液的HPLC分析显示，主要的分解产物是由每个pGlu-X肽去除pGlu后产生的H-X肽。结果表明，pGlu-X肽的肽键对酸的敏感性高于所研究的五种肽中的各种内酰胺键，包括Gn-RH中的色氨酸-丝氨酸键、d-NMU-8中的C末端天冬酰胺-NH2键，以及PH中的天冬氨酸-脯氨酸键，其酸敏感性是众所周知的。因此，使用高浓度水溶性MSA的温和水解可能适用于化学选择性去除pGlu，以便进行结构研究。
• Probing the functional conformation of neuropeptide Y through the design and study of cyclic analogs
  作者：Marlene Bouvier、John W. Taylor

  DOI：10.1021/jm00084a021

  日期：1992.3

  The functional importance of the PP-fold conformation in neuropeptide Y (NPY) was investigated. NPY and N(alpha)-Ac-NPY(10-36), and corresponding cyclic analogues cyclo18,22-[Lys18,Asp22]-NPY and N(alpha)-Ac-cyclo18,22-[Lys18,Asp22]-NPY(10-36), were synthesized. Strategies for synthesis of the cyclic analogues included the use of the Kaiser oxime resin and a segment condensation approach. Circular dichroism studies in phosphate buffer, pH 5.0, indicated self-association of all four peptides at low micromolar concentrations. Monomeric N(alpha)-Ac-NPY(10-36) showed only 13% alpha-helix, compared to 32% alpha-helix for monomeric NPY, demonstrating a helix-stabilizing effect of residues 1-9 that is consistent with the PP fold. The [Lys18,Lys22] lactam bridge stabilized the helical conformation in N(alpha)-Ac-NPY(10-36) (51% alpha-helix), but was helix destabilizing in NPY (21% alpha-helix). In rat brain receptor binding assays, the cyclic and linear N(alpha)-Ac-NPY(10-36) analogues were equipotent (IC50 = 13 nM for I-125-BH-NPY displacement), although the cyclic analogue was twice as potent in rat vas deferens assays. NPY was more potent than its cyclic analogue in the brain receptor binding assays (IC50 = 0.07 and 0.25 nM, respectively), but these peptides were equipotent in the vas deferens assays. These results support a functional role for the PP fold in NPY and correlate with the solution conformations of the monomeric peptides.