H-Val-Tyr-OMe*HCl | 54244-57-4

• 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: H-Val-Tyr-OMe*HCl
• 英文别名: N-L-valyl-L-tyrosine methyl ester; hydrochloride；N-L-Valyl-L-tyrosin-methylester; Hydrochlorid；Valyltyrosine methyl ester hydrochloride；methyl (2S)-2-[[(2S)-2-amino-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoate;hydrochloride
• CAS: 54244-57-4
• 化学式: C₁₅H₂₂N₂O₄*ClH
• 分子量: 330.812
• InChiKey: HLLBFELELLOLAY-QNTKWALQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.0
• 重原子数：
  22
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  102
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  H-Val-Tyr-OMe*HCl 在 盐酸 、 三乙胺 作用下， 以 1,4-二氧六环 、 N,N-二甲基甲酰胺 为溶剂， 反应 48.0h， 生成 Boc-Gln-Tyr-Asp(OBzl)-Val-Tyr-OMe
  参考文献：
  名称：

  Amino acids and peptides. XXVIII. Synthesis of peptide fragments related to eglin c and studies on the relationship between their structure and effects on human leukocyte elastase, cathepsin G and .ALPHA.-chymotrypsin.

  摘要：

  采用常规的溶液法合成了与来自家蚕血淋巴的抗蛋白酶eglin c（由70个氨基酸残基构成）相关的各种肽片段，并检验了它们对白细胞弹性蛋白酶、组织蛋白酶G和α-胰凝乳蛋白酶的抑制效应。其中，H-Arg-Glu-Tyr-Phe-OMe（eglin c 22-25）和H-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-OMe（eglin c 41-49）能抑制组织蛋白酶G和α-胰凝乳蛋白酶，但不能抑制白细胞弹性蛋白酶，而H-Thr-Asn-Val-Val-OMe（eglin c 60-63）能抑制白细胞弹性蛋白酶，但不能抑制组织蛋白酶G或α-胰凝乳蛋白酶，尽管eglin c对白细胞弹性蛋白酶、组织蛋白酶G和α-胰凝乳蛋白酶都具有强抑制作用。这些结果提示，eglin c与白细胞弹性蛋白酶、组织蛋白酶G和α-胰凝乳蛋白酶的相互作用部位可能各不相同。

  DOI：

  10.1248/cpb.38.2369
• 作为产物：
  描述：

  Boc-Val-Tyr-OMe 在 盐酸 作用下， 以 1,4-二氧六环 为溶剂， 生成 H-Val-Tyr-OMe*HCl
  参考文献：
  名称：

  Amino acids and peptides. XXVIII. Synthesis of peptide fragments related to eglin c and studies on the relationship between their structure and effects on human leukocyte elastase, cathepsin G and .ALPHA.-chymotrypsin.

  摘要：

  采用常规的溶液法合成了与来自家蚕血淋巴的抗蛋白酶eglin c（由70个氨基酸残基构成）相关的各种肽片段，并检验了它们对白细胞弹性蛋白酶、组织蛋白酶G和α-胰凝乳蛋白酶的抑制效应。其中，H-Arg-Glu-Tyr-Phe-OMe（eglin c 22-25）和H-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-OMe（eglin c 41-49）能抑制组织蛋白酶G和α-胰凝乳蛋白酶，但不能抑制白细胞弹性蛋白酶，而H-Thr-Asn-Val-Val-OMe（eglin c 60-63）能抑制白细胞弹性蛋白酶，但不能抑制组织蛋白酶G或α-胰凝乳蛋白酶，尽管eglin c对白细胞弹性蛋白酶、组织蛋白酶G和α-胰凝乳蛋白酶都具有强抑制作用。这些结果提示，eglin c与白细胞弹性蛋白酶、组织蛋白酶G和α-胰凝乳蛋白酶的相互作用部位可能各不相同。

  DOI：

  10.1248/cpb.38.2369

文献信息

• Sarcosine.sup.1 dehydroalanine.sup.8 angiotensin II derivatives
  申请人：G. D. Searle & Co.

  公开号：US04204991A1

  公开（公告）日：1980-05-27

  The sarcosine.sup.1 dehydroalanine.sup.8 angiotensin II derivatives of the present invention are potent angiotensin blockers.

  本发明中的肌氨酸衍生物（sarcosine.sup.1 dehydroalanine.sup.8 angiotensin II derivatives）是有效的血管紧张素拮抗剂。
• Exploration of neutral endopeptidase active site by a series of new thiol-containing inhibitors
  作者：Isabel Gomez-Monterrey、Serge Turcaud、Evelyne Lucas、Luce Bruetschy、Bernard P. Roques、Marie Claude Fournie-Zaluski

  DOI：10.1021/jm00053a011

  日期：1993.1

  With the aim of characterizing the active site of the neutral endopeptidase [EC 3.4.24.11 (NEP)] and especially its putative S1 subsite, two series of new thiol inhibitors designed to interact with the S1, S'1, and S'2 subsites of the enzyme have been synthesized. These molecules correspond to the general formula HSCH(R1)CH(R2)CONHCH(R3)COOH (series I) and HSCH(R1)CH(R2)-CONHCH(R3)CONHCH(R4)COOH(series II). Due to the synthetic pathway used, these inhibitors were obtained as mixtures of four stereoisomers. HPLC separation of the stereoisomers of 17 HSCH[CH2CH(CH3)2]CH(CH2Ph)CONHCH(CH3)COOH allowed the stereochemical dependence of the inhibitory potency to be determined. The most active isomer 17b (IC50 = 3.6 nM) is assumed to have the S,S,S stereochemistry as deduced from both NMR and HPLC data. Although none of the inhibitors obtained were significantly more active than thiorphan, HSCH2CH(CH2Ph)-CONHCH2COOH (IC50 = 4 nM), which interacts only with the S'1 and S'2 subsites of NEP, their enhanced hydrophobicity is expected to improve their pharmacokinetic properties. An these compounds displayed low affinities for ACE (IC50s > 1 muM). The determination of the IC50s of two inhibitors of series II for NEP and for a mutated enzyme in which Arg102 was replaced by Glu102 allowed their mode of binding to the active site of NEP to be characterized. The R2 and R3 chains fit the S'1-S'2 subsites, while the R4 group is probably located outside the active site. Taken together these results indicate that the R1 chain of these inhibitors creates no additional stabilizing interactions with the active site of NEP. Two hypotheses may account for this: there is no hydrophobic S1 subsite in NEP or the inhibitors have structures which are too constrained for optimized interactions with the active site.
• TSUBOI, SATOSHI;NAKABAYASHI, KAZUNORI;MATSUMOTO, YOSHIKAZU;TENO, NAOKI;TS+, CHEM. AND PHARM. BULL., 38,(1990) N, C. 2369-2376
  作者：TSUBOI, SATOSHI、NAKABAYASHI, KAZUNORI、MATSUMOTO, YOSHIKAZU、TENO, NAOKI、TS+

  DOI：——

  日期：——
• US4204991A
  申请人：——

  公开号：US4204991A

  公开（公告）日：1980-05-27