Ac-AGSRHWKFL-NH₂ | 1422521-01-4

• 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: Ac-AGSRHWKFL-NH₂
• 英文别名: Ac-Ala-Gly-Ser-Arg-His-Trp-Lys-Phe-Leu-NH2；(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-acetamidopropanoyl]amino]acetyl]amino]-3-hydroxypropanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-6-amino-N-[(2S)-1-[[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]amino]-1-oxo-3-phenylpropan-2-yl]hexanamide
• CAS: 1422521-01-4
• 化学式: C₅₄H₇₉N₁₇O₁₁
• 分子量: 1142.33
• InChiKey: QCLPTSFAGAMWNW-XTBCULCOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.6
• 重原子数：
  82
• 可旋转键数：
  35
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.48
• 拓扑面积：
  460
• 氢给体数：
  16
• 氢受体数：
  14

反应信息

• 作为反应物：
  描述：

  Ac-AGSRHWKFL-NH₂ 在 nickel(II) chloride hexahydrate 、 水 、 三氟乙酸 作用下， 以 水 为溶剂， 反应 8.0h， 生成 (S)-6-amino-2-((S)-2-((S)-2-((S)-2-((S)-2-amino-3-hydroxypropanamido)-5-guanidinopentanamido)-3-(1H-imidazol-5-yl)propanamido)-3-(1H-indol-3-yl)propanamido)-N-((S)-1-(((S)-1-amino-4-methyl-1-oxopentan-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)hexanamide 、
  参考文献：
  名称：

  Effect of d-Amino Acid Substitutions on Ni(II)-Assisted Peptide Bond Hydrolysis

  摘要：

  Previously we demonstrated the sequence-specific hydrolysis of the R-1-(Ser/Thr)-peptide bond in Ni(II) complexes of peptides with a general R-1-(Ser/Thr)-Xaa-His-Zaa-R-2 sequence (R-1 and R-2 being any sequences) (Kopera, E.; Krezel, A.; Protas, A. M.; Belczyk, A.; Bonna, A.; Wyslouch-Cieszynska, A.; Poznanski, J.; Bal, W. Inorg. Chem. 2010, 49, 6636). In order to refine our understanding of the mechanism of this reaction and to find ways to accelerate it, we undertook a systematic study of effects of D-amino acid substitutions in the template Ac-Gly-Ala-Ser-Arg-His-Trp-Lys-Phe-Leu-NH2 peptide on the hydrolysis rate constants. We found that all stereochemical alterations made around the Ni(II) chelate plane resulted in the decrease of the reaction rate. However, the Ni(II) coordination, a prerequisite to the reaction, was not compromised by these substitutions. We demonstrated that the reaction is only possible when either the side chain of the crucial Ser (or Thr) residue is on the same part of the chelate plane as the next residue in the sequence (Arg), or the side chain of the residue following His (Trp) resides on the opposite side of the plane. The rate of reaction is the fastest when both these conditions are fulfilled. Another novel effect is the strong dependence of the rate of the acyl shift step on the character of the leaving group.

  DOI：

  10.1021/ic3022672

文献信息

• Effect of <scp>d</scp>-Amino Acid Substitutions on Ni(II)-Assisted Peptide Bond Hydrolysis
  作者：Hanieh H. Ariani、Agnieszka Polkowska-Nowakowska、Wojciech Bal

  DOI：10.1021/ic3022672

  日期：2013.3.4

  Previously we demonstrated the sequence-specific hydrolysis of the R-1-(Ser/Thr)-peptide bond in Ni(II) complexes of peptides with a general R-1-(Ser/Thr)-Xaa-His-Zaa-R-2 sequence (R-1 and R-2 being any sequences) (Kopera, E.; Krezel, A.; Protas, A. M.; Belczyk, A.; Bonna, A.; Wyslouch-Cieszynska, A.; Poznanski, J.; Bal, W. Inorg. Chem. 2010, 49, 6636). In order to refine our understanding of the mechanism of this reaction and to find ways to accelerate it, we undertook a systematic study of effects of D-amino acid substitutions in the template Ac-Gly-Ala-Ser-Arg-His-Trp-Lys-Phe-Leu-NH2 peptide on the hydrolysis rate constants. We found that all stereochemical alterations made around the Ni(II) chelate plane resulted in the decrease of the reaction rate. However, the Ni(II) coordination, a prerequisite to the reaction, was not compromised by these substitutions. We demonstrated that the reaction is only possible when either the side chain of the crucial Ser (or Thr) residue is on the same part of the chelate plane as the next residue in the sequence (Arg), or the side chain of the residue following His (Trp) resides on the opposite side of the plane. The rate of reaction is the fastest when both these conditions are fulfilled. Another novel effect is the strong dependence of the rate of the acyl shift step on the character of the leaving group.