H-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-OH | 122299-11-0

• 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-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-OH
• 英文别名: (3S)-3-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-amino-3-hydroxypropanoyl]pyrrolidine-2-carbonyl]amino]-3-methylbutanoyl]amino]-3-hydroxybutanoyl]amino]-4-methylpentanoyl]amino]-4-[[(2S)-1-[[(2S)-1-[[(1S)-1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-4-oxobutanoic acid
• CAS: 122299-11-0
• 化学式: C₄₈H₇₈N₁₂O₁₅
• 分子量: 1063.22
• InChiKey: LMIACVIHSZIJKT-WWRYCTMDSA-N

物化性质

• 密度：
  1.44±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -3.6
• 重原子数：
  75
• 可旋转键数：
  31
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.65
• 拓扑面积：
  450
• 氢给体数：
  15
• 氢受体数：
  17

反应信息

• 作为产物：
  描述：

  Boc-Ser-Pro-Val-Thr-Leu-Asp(OBzl)-Leu-Arg(Mts)-Tyr-OBzl 在 茴香硫醚 、 氢氟酸 、 间甲酚 作用下， 反应 1.5h， 以83%的产率得到H-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-OH
  参考文献：
  名称：

  Amino acids and peptides. XXX. Synthesis of eglin c(41-49) and eglin c(60-63) and examination of their inhibitory activity towards human leukocyte elastase, cathepsin G, porcine pancreatic elastase and .ALPHA.-chymotrypsin.

  摘要：

  H-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-OH 和 H-Thr-Asn-Val-Val-OH 分别对应于 eglin c 的序列 41-49 和 60-63，通过采用新开发的 6-氯-2-吡啶酯方法，使用常规溶液法合成。以上两种肽对人类白细胞弹性蛋白酶、半胱天冬酶 G、猪胰弹性蛋白酶和 α-化学蛋白酶的抑制活性进行了比较，分析其与相应甲基酯的活性差异。

  DOI：

  10.1248/cpb.39.184

文献信息

• Amino acids and peptides. XXX. Synthesis of eglin c(41-49) and eglin c(60-63) and examination of their inhibitory activity towards human leukocyte elastase, cathepsin G, porcine pancreatic elastase and .ALPHA.-chymotrypsin.
  作者：Satoshi TSUBOI、Miho TAKEDA、Yoshio OKADA、Yoko NAGAMATSU、Junichiro YAMAMOTO

  DOI：10.1248/cpb.39.184

  日期：——

  H-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-OH and H-Thr-Asn-Val-Val-OH, which correspond to the sequences 41-49 and 60-63 of eglin c, respectively, were synthesized by a conventional solution approach using the newly developed 6-chloro-2-pyridyl ester method. The inhibitory activities of the above two peptides against human leukocyte elastase, cathepsin G, porcine pancreatic elastase and α-chymotrypsin were examined in comparison with those of the corresponding methyl esters.

  H-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-OH 和 H-Thr-Asn-Val-Val-OH 分别对应于 eglin c 的序列 41-49 和 60-63，通过采用新开发的 6-氯-2-吡啶酯方法，使用常规溶液法合成。以上两种肽对人类白细胞弹性蛋白酶、半胱天冬酶 G、猪胰弹性蛋白酶和 α-化学蛋白酶的抑制活性进行了比较，分析其与相应甲基酯的活性差异。
• TSUBOI, SATOSHI;TAKEDA, MIHO;OKADA, YOSHIO;NAGAMATSU, YOKO;YAMAMOTO, JUNI+, CHEM. AND PHARM. BULL., 39,(1991) N, C. 184-186
  作者：TSUBOI, SATOSHI、TAKEDA, MIHO、OKADA, YOSHIO、NAGAMATSU, YOKO、YAMAMOTO, JUNI+

  DOI：——

  日期：——
• Amino Acids and Peptides. XXXVII. Synthesis of Stereoisomeric Nonapeptides Corresponding to Sequence 41-49 of Eglin c and Examination of Their Inhibitory Activity against Human Leukocyte Cathepsin G and .ALPHA.-Chymotrypsin.
  作者：Ayumi FUJII、Satoshi TSUBOI、Keiichi ASADA、Yoko NAGAMATSU、Junichiro YAMAMOTO、Yoshio OKADA

  DOI：10.1248/cpb.42.1518

  日期：——

  A nonapeptide, H-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-OH, corresponding to sequence 41-49 of eglin c inhibited leukocyte cathepsin G and α-chymotrypsin with Ki values of 2.2×10-5 and 7.2×10-6M, respectively, although eglin c itself inhibited leukocyte elastase, cathepsin G and α-chymotrypsin with Ki values of 6.0×10-9, 5.5×10-9 and 2.5×10-9M, respectively. The inhibitory activity of the nonapeptide decreased following incubation with cathepsin G due to the cleavage of the Leu45-Asp46 peptide bond. Therefore, Leu45 and/or Asp46 were replaced with D-amino acids and the inhibitory activities of the resultant nonapeptides were examined. Their inhibitory activities against cathepsin G and α-chymotrypsin were much weaker than those of the all-L-type nonapeptide, suggesting that the amino acids at the active site, Leu45 and Asp46 are required to be in the L-configuration for potent activity.

  一种非apeptide，H-Ser-Pro-Val-Thr-Leu-Asp-Leu-Arg-Tyr-OH，对应于eglin c序列41-49，分别以2.2×10-5和7.2×10-6M的Ki值抑制白细胞组织蛋白酶G和α-胰凝乳蛋白酶，尽管eglin c本身分别以6.0×10-9、5.5×10-9和2.5×10-9M的Ki值抑制白细胞弹性蛋白酶、组织蛋白酶G和α-胰凝乳蛋白酶。非apeptide的抑制活性在与组织蛋白酶G孵育后下降，这是由于Leu45-Asp46肽键的断裂。因此，Leu45和/或Asp46被替换为D-氨基酸，并对产生的非apeptide的抑制活性进行了检查。它们对组织蛋白酶G和α-胰凝乳蛋白酶的抑制活性远弱于所有L型非apeptide，表明活性位点上的氨基酸，Leu45和Asp46，需要处于L-构型才能发挥强大活性。