[Pd(ONO2)2((15)NH2CH2CH2(15)NH2)] | 558480-98-1

• 分子结构分类: 无机化合物
• 英文名称: [Pd(ONO2)2((15)NH2CH2CH2(15)NH2)]
• 英文别名: [Pd(en)(ONO2)2]；[Pd(15en)(ONO2)2]
• CAS: 558480-98-1
• 化学式: C₂H₈N₄O₆Pd
• 分子量: 292.515
• InChiKey: XCJQGMIFFWZHDI-SFXOSDSGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  None
• 重原子数：
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• 可旋转键数：
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• 环数：
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• sp3杂化的碳原子比例：
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• 拓扑面积：
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• 氢给体数：
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• 氢受体数：
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反应信息

• 作为反应物：
  描述：

  [Pd(ONO2)2((15)NH2CH2CH2(15)NH2)] 在 水 作用下， 以 水 为溶剂， 生成 diaqua(ethylenediamine-(15)N2)palladium(II) nitrate
  参考文献：
  名称：

  Appleton, Trevor G.; Bailey, Alicia J.; Bedgood Jr., Danny R., Inorganic Chemistry, 1994, vol. 33, # 2, p. 217 - 226

  摘要：

  DOI：
• 作为产物：
  描述：

  dichloro(ethylenediamine-(15)N2)palladium 、 silver nitrate 以 水 为溶剂， 以73%的产率得到[Pd(ONO2)2((15)NH2CH2CH2(15)NH2)]
  参考文献：
  名称：

  Ma, Michelle T.; Hoang, Huy N.; Scully, Conor C. G., Journal of the American Chemical Society, 2009, vol. 131, p. 4505 - 4512

  摘要：

  DOI：

文献信息

• Linkage Isomerism in the Binding of Pentapeptide Ac-His(Ala)₃His-NH₂ to (Ethylenediamine)Palladium(II): Effect of the Binding Mode on Peptide Conformation
  作者：Huy N. Hoang、Gavin K. Bryant、Michael J. Kelso、Renee L. Beyer、Trevor G. Appleton、David P. Fairlie

  DOI：10.1021/ic800970p

  日期：2008.10.20

  linkage isomer of 2 was not observed. Complex 10 was also the major product in aqueous solution, but other species were also present. All compounds were exhaustively characterized in solution by multinuclear 1D ((1)H , (13)C, and, with (15)N-labeled ethylenediamine, (15)N) and 2D (correlation spectroscopy, total correlation spectroscopy, transverse rotating-frame Overhauser effect spectroscopy (T-ROESY)

  五肽Ac-His1-Ala2-Ala3-Ala4-His5-NH2（AcHAAAHNH2）（1）与[Pd（en）（ONO2）2]（en = NH2CH2CH2NH2）在DMF-d（7）或H2O中的反应：D2O（90％：10％）得到[Pd（en）（AcHAAAHNH2）]（2+）（2），2a，2b和2c的三个键合异构体，其区别仅在于咪唑氮原子对与Pd。在最丰富的异构体2a中，Pd与来自两个咪唑环中每个环的N1键合。在次要异构体2b和2c中，Pd分别与N1（His1）和N3（His5）以及N3（His1）和N1（His5）结合。[Pd（en）（ONO2）2]与N-甲基化肽Ac-（N3-MeHis）-Ala-Ala-Ala-（N3-MeHis）-NH2（AcH * AAAH * NH2）的反应（3） ，Ac-（N3-MeHis）-Ala-Ala-Ala-（N1-MeHis）-NH2（AcH（*）
• α-Turn Mimetics:  Short Peptide α-Helices Composed of Cyclic Metallopentapeptide Modules
  作者：Michael J. Kelso、Renée L. Beyer、Huy N. Hoang、Ami S. Lakdawala、James P. Snyder、Warren V. Oliver、Tom A. Robertson、Trevor G. Appleton、David P. Fairlie

  DOI：10.1021/ja037980i

  日期：2004.4.1

  alpha-Helices are key structural components of proteins and important recognition motifs in biology. Short peptides (less than or equal to15 residues) corresponding to these helical sequences are rarely helical away from their stabilizing protein environments. New techniques for stabilizing short peptide helices could be valuable for studying protein folding, modeling proteins, creating artificial proteins, and may aid the design of inhibitors or mimics of protein function. This study reports the facile incorporation of 3- and 4-alpha turns in 10-15 residue peptides through formation in situ of multiple cyclic metallopeptide modules [Pd(en)(H*XXXH*)](2+). The nonhelical peptides Ac-H*ELTH*H*VTDH*-NH2 (1), Ac-H*ELTH*AVTDYH*ELTH*-NH2 (2), and Ac-H*AAAH*H*ELTH*H*VTDH*-NH2 (3) (H* is histidine-methylated at imidazole-N3) react in N,N-dimethylformamide (DMF) or water with 2, 2, and 3 molar equivalents, respectively, of [Pd(en)(NO3)(2)] to form exclusively [Pd-2(en)(2)(Ac-H*ELTH*H*VTDH*-NH2)](4+) (4), [Pd-2(en)(2)(Ac-H*ELTH*AVTDYH*ELTH*-NH2)](4+) (5), and [Pd-3(en)(3)(Ac-H*AAAH*H*ELTH*H*VTDH*-NH2)](6+) (6), characterized by mass spectrometry, 1D and 2D H-1- and 1D N-15-NMR spectroscopy. Despite the presence of multiple histidines and other possible metal-binding residues in these peptides, 2D H-1 NMR spectra reveal that Pd(en)(2+) is remarkably specific in coordinating to imidazole-N1 of only (i, i + 4) pairs of histidines (i.e., only those separated by three amino acids), resulting in 4-6 made up of cyclic metallopentapeptide modules ([Pd(en)(H*XXXH*)](2+))(n), n = 2, 2, 3, respectively, each cycle being a 22-membered ring. We have previously shown that a single metallopentapeptide can nucleate alpha-helicity (Kelso et al., Angew. Chem., Int. Ed. 2003, 42, 421-424.). We now demonstrate its use as an alpha-turn-mimicking module for the facile conversion of unstructured short peptides into helices of macrocycles and provide 1D and 2D NMR spectroscopic data, structure calculations via XPLOR and NMR analysis of molecular flexibility in solution (NAMFIS), and CD spectra in support of the alpha-helical nature of these monomeric metallopeptides in solution.
• Metal Clips Induce Folding of a Short Unstructured Peptide into an α-Helix via Turn Conformations in Water. Kinetic versus Thermodynamic Products
  作者：Renée L. Beyer、Huy N. Hoang、Trevor G. Appleton、David P. Fairlie

  DOI：10.1021/ja0453782

  日期：2004.11.1

  Short peptides corresponding to two to four a-helical turns of proteins are not thermodynamically stable helices in water. Unstructured octapeptide Ac-His1*-Ala2-Ala3-His4*-His5*-Glu6-Leu7-His8*-NH2 (1) reacts with two [Pd ((NH2)-N-15(CH2)(2) (NH2)-N-15)(NO3)(2)] in water to form a kinetically stable intermediate, [Pden}(2)-(1,4)(5,8)-peptide}](2), in which two 19-membered metallocyclic rings stabilize two peptide turns. Slow subsequent folding to a thermodynamically more stable two-turn a-helix drives the equilibrium to [Pden}(2)-(1,5)(4,8)-peptide}] (3), featuring two 22-membered rings. This transformation from unstructured peptide via turns to an a-helix suggests that metal clips might be useful probes for investigating peptide folding.
• A Cyclic Metallopeptide Induces α Helicity in Short Peptide Fragments of Thermolysin
  作者：Michael J. Kelso、Huy N. Hoang、Warren Oliver、Nikolai Sokolenko、Darren R. March、Trevor G. Appleton、David P. Fairlie

  DOI：10.1002/anie.200390128

  日期：2003.1.27