MDCSGCSRPG | 1426823-98-4

• 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: MDCSGCSRPG
• 英文别名: cyclo[Arg-Pro-Gly-Met-Asp-Cys-Ser-Gly-Cys-Ser]；2-[(3S,6S,9R,15S,18R,21S,24S,30S)-3-[3-(diaminomethylideneamino)propyl]-6,15-bis(hydroxymethyl)-24-(2-methylsulfanylethyl)-2,5,8,11,14,17,20,23,26,29-decaoxo-9,18-bis(sulfanylmethyl)-1,4,7,10,13,16,19,22,25,28-decazabicyclo[28.3.0]tritriacontan-21-yl]acetic acid
• CAS: 1426823-98-4
• 化学式: C₃₆H₅₉N₁₃O₁₄S₃
• 分子量: 994.141
• InChiKey: DKHMMJKXIPGGCN-OPKHLUCYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -5.6
• 重原子数：
  66
• 可旋转键数：
  13
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  452
• 氢给体数：
  16
• 氢受体数：
  18

反应信息

• 作为反应物：
  描述：

  MDCSGCSRPG 、 zinc(II) chloride 以 水 、 氘代二甲亚砜 为溶剂， 生成
  参考文献：
  名称：

  Peptide Models of Cu(I) and Zn(II) Metallochaperones: The Effect of pH on Coordination and Mechanistic Implications

  摘要：

  The first NMR structures of Cu(I) and Zn(II) peptide complexes as models of metallochaperones were derived with no predetermined binding mode. The cyclic peptide MDCSGCSRPG was reacted with Cu(I) and Zn(II) at low and moderate pH. This peptide features the conserved sequence of copper chaperones but with Asp at position 2 as appears in the zinc binding domain of ZntA. The structures were compared with those of the Cu(I) complexes of the wildtype sequence peptide MTCSGCSRPG. All analyses were conducted first with no metal-binding constraints to ensure accurate binding ligand assignment. Several structures included metal-Met binding, raising a possible role of Met in the metal transport mechanism. Both Cu(I) and Zn(II) gave different complexes when reacted with the peptide of the native-like sequence under different pH conditions, raising the possibility of pH-dependent transport mechanisms. Cu(I) bound the MTCSGCSRPG peptide through one Cys and the Met under acidic conditions and differently under basic conditions; Zn(II) bound the MDCSGCSRPG peptide through two Cys and the Met residues under acidic conditions and through one Cys and the Met under basic conditions, while Cu(I) bound the non-native Asp mutant peptide through the Asp and one Cys under both conditions, suggesting that Asp may inhibit pH-dependent binding for Cu(I). NOESY and ESI-HRMS supported the presence of an aqua ligand for Zn(II), which likely deprotonated under basic conditions to give a hydroxo group. Coordination similarities were detected among the model system and native proteins, which overall suggest that coordination flexibility is required for the function of metallochaperones.

  DOI：

  10.1021/ic302404w

文献信息

• Peptide Models of Cu(I) and Zn(II) Metallochaperones: The Effect of pH on Coordination and Mechanistic Implications
  作者：Michal S. Shoshan、Deborah E. Shalev、Edit Y. Tshuva

  DOI：10.1021/ic302404w

  日期：2013.3.18

  The first NMR structures of Cu(I) and Zn(II) peptide complexes as models of metallochaperones were derived with no predetermined binding mode. The cyclic peptide MDCSGCSRPG was reacted with Cu(I) and Zn(II) at low and moderate pH. This peptide features the conserved sequence of copper chaperones but with Asp at position 2 as appears in the zinc binding domain of ZntA. The structures were compared with those of the Cu(I) complexes of the wildtype sequence peptide MTCSGCSRPG. All analyses were conducted first with no metal-binding constraints to ensure accurate binding ligand assignment. Several structures included metal-Met binding, raising a possible role of Met in the metal transport mechanism. Both Cu(I) and Zn(II) gave different complexes when reacted with the peptide of the native-like sequence under different pH conditions, raising the possibility of pH-dependent transport mechanisms. Cu(I) bound the MTCSGCSRPG peptide through one Cys and the Met under acidic conditions and differently under basic conditions; Zn(II) bound the MDCSGCSRPG peptide through two Cys and the Met residues under acidic conditions and through one Cys and the Met under basic conditions, while Cu(I) bound the non-native Asp mutant peptide through the Asp and one Cys under both conditions, suggesting that Asp may inhibit pH-dependent binding for Cu(I). NOESY and ESI-HRMS supported the presence of an aqua ligand for Zn(II), which likely deprotonated under basic conditions to give a hydroxo group. Coordination similarities were detected among the model system and native proteins, which overall suggest that coordination flexibility is required for the function of metallochaperones.