[Phe(p-guanidine)5]SFTI-1 | 1161949-07-0

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: [Phe(p-guanidine)5]SFTI-1
• 英文别名: H-Gly-Arg-Cys(1)-Thr-Phe(4-guanidino)-Ser-Ile-Pro-Pro-Ile-Cys(1)-Phe-Pro-Asp-OH；(2S)-2-[[(2S)-1-[(2S)-2-[[(3S,9S,12S,15S,18S,21R,26R,29S,32S)-21-[[(2S)-2-[(2-aminoacetyl)amino]-5-(diaminomethylideneamino)pentanoyl]amino]-9,29-bis[(2S)-butan-2-yl]-15-[[4-(diaminomethylideneamino)phenyl]methyl]-18-[(1R)-1-hydroxyethyl]-12-(hydroxymethyl)-2,8,11,14,17,20,28,31-octaoxo-23,24-dithia-1,7,10,13,16,19,27,30-octazatricyclo[30.3.0.03,7]pentatriacontane-26-carbonyl]amino]-3-phenylpropanoyl]pyrrolidine-2-carbonyl]amino]butanedioic acid
• CAS: 1161949-07-0
• 化学式: C₇₁H₁₀₆N₂₀O₁₉S₂
• 分子量: 1607.88
• InChiKey: RAWTVOJXKLIRQY-XNFZKIEOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.4
• 重原子数：
  112
• 可旋转键数：
  27
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  672
• 氢给体数：
  19
• 氢受体数：
  24

反应信息

• 作为产物：
  描述：

  在 碘 作用下， 以 甲醇 为溶剂， 生成 [Phe(p-guanidine)5]SFTI-1
  参考文献：
  名称：

  Introduction of non-natural amino acid residues into the substrate-specific P1 position of trypsin inhibitor SFTI-1 yields potent chymotrypsin and cathepsin G inhibitors

  摘要：

  A series of trypsin inhibitor SFTI-1 compounds modified in substrate-specific P-1 position was synthesized by the solid-phase method. Lys5 present in the wild inhibitor was replaced by Phe derivatives substituted in para position of the phenyl ring, L-pyridylalanine and N-4-nitrobenzylgycine. Their inhibitory activities with bovine alpha-chymotrypsin and cathepsin G were estimated by determination of association equilibrium constants (K-a). All analogues inhibited bovine alpha-chymotrypsin. The highest inihbitory activity displayed peptides with the fluorine, nitro and methyl substituents. They were 13-15-fold more active than [Phe(5)] SFTI-1 used as a reference. They are the most potent chymotrypsin inhibitors of this size. Substitution of Lys5 by Phe did not change the cathepsin G inhibitory activity. Introduction of Phe( p-F), Phe (p-NH2) and Phe(p-CH3) in this position retained the affinity towards this proteinase, whereas Phe(p-guanidine) gave an inhibitor more than twice as active, which appeared to be stable in human serum. On the other hand, a peptomeric analogue with N-4-nitrobenzylglycine failed to inhibit cathepsin G. Despite the fact the introduced amino acids were non-coded, the peptide bonds formed by them were hydrolyzed by chymotrypsin. We postulate that additional interaction of para-substitutents with the enzyme are responsible for the enhanced inhibitory activity of the analogues. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2009.03.045