血管紧张素II(1-4),人 | 52580-29-7

• 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
• 中文名称: 血管紧张素II(1-4),人
• 英文名称: Asp-Arg-Val-Tyr
• 英文别名: L-Asp-L-Arg-L-Val-L-Tyr；DRVY；Angiotensin II (1-4), human；(3S)-3-amino-4-[[(2S)-1-[[(2S)-1-[[(1S)-1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-4-oxobutanoic acid
• CAS: 52580-29-7
• 化学式: C₂₄H₃₇N₇O₈
• 分子量: 551.6
• InChiKey: KFWYCVYZWAMJRF-DWRORGKVSA-N

物化性质

• 溶解度：
  溶于二甲基亚砜

计算性质

• 辛醇/水分配系数(LogP)：
  -5.3
• 重原子数：
  39
• 可旋转键数：
  16
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  273
• 氢给体数：
  9
• 氢受体数：
  10

制备方法与用途

生物活性

Angiotensin II (1-4), human 是一种由 AT I 经血管紧张素转换酶(ACE)合成的内源性多肽。它与 AT II 1 型 (AT1) 受体结合，刺激血管平滑肌细胞中的 GPCRs，增加细胞内的 Ca2+ 水平。此外，Angiotensin II 还在肾小管近端的 Na+/H+ 交换器中发挥作用。

多肽

Angiotensin II (1-4), human 是一种由 AT I 经血管紧张素转换酶(ACE)合成的内源性多肽，含有四个氨基酸。它与 AT II 1 型 (AT1) 受体结合，刺激血管平滑肌细胞中的 GPCRs，增加细胞内的 Ca2+ 水平。此外，Angiotensin II 还在肾小管近端的 Na+/H+ 交换器中发挥作用。

参考质量标准

• 外观：白色粉末
• 纯度 (HPLC) ≥98.0%
• 醋酸根含量 ≤12.0%
• 水分含量 ≤8.0%
• 肽含量 ≥80.0%
• 内毒素 ≤50EU/mg
• 氨基酸组成分析 ≤±10%

上下游信息

• 上游原料

  中文名称	英文名称	CAS号	化学式	分子量
  血管紧张素 I	angiotensin I	484-42-4	C62H89N17O14	1296.49

反应信息

• 作为产物：
  描述：

  血管紧张素 I 在 recombinant human kallikrein-related peptidase 3 、 sodium citrate 作用下， 反应 1.0h， 生成 IHPFHL 、 血管紧张素II(1-4),人
  参考文献：
  名称：

  Substrate specificity and inhibition of human kallikrein-related peptidase 3 (KLK3 or PSA) activated with sodium citrate and glycosaminoglycans

  摘要：

  We report the enzymatic properties and substrate specificity of human recombinant KLK3 in the presence of glycosaminoglycans (GAGs) and sodium citrate. This salt is highly concentrated in prostate and in its presence KLK3 had a similar hydrolytic efficiency as chymotrypsin. In contrast to the latter peptidase. KLK3 activated by sodium citrate efficiently hydrolyzed substrates containing R, H and Pat the P1 position. Activated KLK3 also cleaved peptides derived from the bradykinin domain of human kininogen at the same sites as human kallikrein KLK1, but presented low kininogenase activity. Angiotensin I has several sites for hydrolysis by KLK3; however, it was cleaved only at the Y-I bond (DRVY down arrow IHPFHL). Sodium citrate modulated KLK3 conformation as observed by alterations to the intrinsic fluorescence of phenylalanines and tryptophans. Activated KLK3 was reversibly inhibited by Z-Pro-Prolinal and competitively inhibited by ortho-phenantroline. Together, these are noteworthy observations for the future design of specific non-peptide inhibitors of KLK3 and to find natural substrates. (c) 2010 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.abb.2010.03.022

文献信息

• Substrate specificity and inhibition of human kallikrein-related peptidase 3 (KLK3 or PSA) activated with sodium citrate and glycosaminoglycans
  作者：Douglas Andrade、Diego M. Assis、Aurelio Resende Lima、Juliana R. Oliveira、Mariana S. Araujo、Sachiko I. Blaber、Michael Blaber、Maria A. Juliano、Luiz Juliano

  DOI：10.1016/j.abb.2010.03.022

  日期：2010.6

  We report the enzymatic properties and substrate specificity of human recombinant KLK3 in the presence of glycosaminoglycans (GAGs) and sodium citrate. This salt is highly concentrated in prostate and in its presence KLK3 had a similar hydrolytic efficiency as chymotrypsin. In contrast to the latter peptidase. KLK3 activated by sodium citrate efficiently hydrolyzed substrates containing R, H and Pat the P1 position. Activated KLK3 also cleaved peptides derived from the bradykinin domain of human kininogen at the same sites as human kallikrein KLK1, but presented low kininogenase activity. Angiotensin I has several sites for hydrolysis by KLK3; however, it was cleaved only at the Y-I bond (DRVY down arrow IHPFHL). Sodium citrate modulated KLK3 conformation as observed by alterations to the intrinsic fluorescence of phenylalanines and tryptophans. Activated KLK3 was reversibly inhibited by Z-Pro-Prolinal and competitively inhibited by ortho-phenantroline. Together, these are noteworthy observations for the future design of specific non-peptide inhibitors of KLK3 and to find natural substrates. (c) 2010 Elsevier Inc. All rights reserved.