Z-Gly-Ser-hydrazide | 19526-00-2

• 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: Z-Gly-Ser-hydrazide
• 英文别名: Benzyloxycarbonylglycyl-L-seryl-hydrazid；Benzyloxycarbonylglycyl-L-serylhydrazid；Z-Gly-Ser-NHNH2；(N-(Benzyloxycarbonyl)glycyl)-l-serine hydrazide；benzyl N-[2-[[(2S)-1-hydrazinyl-3-hydroxy-1-oxopropan-2-yl]amino]-2-oxoethyl]carbamate
• CAS: 19526-00-2
• 化学式: C₁₃H₁₈N₄O₅
• 分子量: 310.31
• InChiKey: BBMCLKGYKDYJLF-JTQLQIEISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.3
• 重原子数：
  22
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.31
• 拓扑面积：
  143
• 氢给体数：
  5
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  Z-Gly-Ser-hydrazide 在 ruthenium trichloride 、 sodium periodate 作用下， 以 四氯化碳 、 乙腈 为溶剂， 反应 4.5h， 生成 Z-Gly-NH-CO-CO-Gly-OMe
  参考文献：
  名称：

  Protein Backbone Modification by Novel C.alpha.-C Side-Chain Scission

  摘要：

  alpha-Ketoamide (-NH-CO-CO-) units in intact peptides are generated from Ser/Thr residues via Ru(VIII)catalyzed C-alpha-C side-chain scission. Facets associated with this novel cu-carbon modification have been probed with 75 peptides chosen to represent every possible peptide environment. The reactions were carried out at room temperature with in situ generated Ru(VIII) in biphasic (CH3CN/CCl4/pH 3 phosphate buffer, 1:1:2 v/v) medium. Whereas Ser/Thr residues placed at the C-terminal end in peptides undergo N-C bond scission leading to des-Ser/Thr peptide amides-thus acting as Gly equivalents in simulating the alpha-amidating action of pituitary enzymes-those located at the N-terminal or nonterminal or even at the C-terminal position (protected as amide) were found to undergo oxidative C-C bond scission (involving C-alpha and C side-chain bond), resulting in the generation of alpha-ketoamide (-NH-CO-CO-) units in the intact peptide backbone. The difference in the products arising from C-alpha-C side-chain scission of Ser/Thr esters and amides is rationalized on the basis of a common mechanism involving either oxaloesters [Pep-NH-CO-COX; X = OMe] or oxalamides [X = NH2 or NH-Pep] arising from the oxidation of initially formed carbinolamide intermediates [Pep-NH-CH(OH)-COX],wherein, while the former are shown to undergo hydrolysis to terminal amides [Pep-NH2], the oxalamides are found to be stable to hydrolysis. Ancillary noteworthy findings are those of peptide bond scission when contiguous Ser-Ser/Thr-Thr residues are present and the oxidative cleavage at C-terminal Tyr/Trp sites generating des amides. The oxidative methodology presented here is mild, simple, and practical and proceeds with chiral retention. The insensitivity of a large number of amino acid residues, such as Gly, Ala, Leu, Asn, Gln, Asp, Glu, Pro, Arg, Phe, Lys, Val, and Aib, and N-protecting groups, such as Boc, Z, and Bz, toward Ru(VIII) under the experimental conditions should make this methodology practical and useful. Sulfur-containing amino acids Cys and Met get oxidized to sulfones in the products.

  DOI：

  10.1021/ja00094a008
• 作为产物：
  描述：

  N-(N-benzyloxycarbonyl-glycyl)-L-serine methyl ester 在 一水合肼 作用下， 以 乙醇 为溶剂， 生成 Z-Gly-Ser-hydrazide
  参考文献：
  名称：

  丝氨酸肽的选择性裂解

  摘要：

  N-苄氧羰基-L-丙氨酰-L-丝氨酸甲酯(I)用光气处理得到相应的O-氯羰基衍生物(II)，然后将其环化为甲基L-3-(N-苄氧羰基-L-丙氨酰)-2-氧代-恶唑烷-4-羧酸酯 (III) 与 N-苄氧羰基-L-丙氨酰-3-氯-L-丙氨酸甲酯 (IV) 在二甲苯中回流。通过 III 的温和碱性水解，N-苄氧羰基-L-丙氨酸和 L-2-氧代-恶唑烷-4-羧酸 (V) 由于肽键的选择性裂解而分离，其中氨基丝氨酸残基参与了。这种方法也适用于其他三种丝氨酸肽；得到了同样的结果。

  DOI：

  10.1246/bcsj.41.974

文献信息

• The Structure of Viscosin, A Peptide Antibiotic. II. Syntheses of D-and L-3-Hydroxyacylhexapeptides including the Proposed Structure of Viscosin and Its Optical Isomers
  作者：MINORU HIRAMOTO、KOZO OKADA、SOTOO NAGAI

  DOI：10.1248/cpb.19.1315

  日期：——

  Homologs of D- and L-3-hydroxyacylhexapeptide including compound (I-1c) and its optical isomers (I-1'c, I-2c, I-2'c) were synthesized by condensing the tripeptide subunit with the dipeptide subunit followed by azide coupling of the resulting pentapeptide with D-or L-3-hydroxyacylleucine, and their antibacterial properties were examined. None of the synthetic acylhexapeptides was identical with viscosin in both physical and chemical properties and antituberculous activity.

  通过将三肽亚基与二肽亚基缩合，然后将得到的五肽与 D-或 L-3-羟乙基亮氨酸叠氮偶联，合成了 D-和 L-3-羟乙基六肽的同系物，包括化合物（I-1c）及其光学异构体（I-1'c、I-2c、I-2'c），并考察了它们的抗菌特性。合成的酰基六肽在理化性质和抗结核活性方面都与粘多糖没有相同之处。
• Selective Cleavage of Serine Peptides
  作者：Takeo Kaneko、Ikuko Takeuchi、Toshishige Inui

  DOI：10.1246/bcsj.41.974

  日期：1968.4

  N-benzyloxycarbonyl-L-alanyl-L-serine methyl ester (I) with phosgene afforded the corresponding O-chlorocarbonyl derivative (II), which was then cyclized to methyl L-3-(N-benzyloxycarbonyl-L-alanyl)-2-oxo-oxazolidine-4-carboxylate (III) accompanied with N-benzyloxycarbonyl-L-alanyl-3-chloro-L-alanine methyl ester (IV) by refluxing in xylene. By the mild alkaline hydrolysis of III, N-benzyloxycarbonyl-L-alanine

  N-苄氧羰基-L-丙氨酰-L-丝氨酸甲酯(I)用光气处理得到相应的O-氯羰基衍生物(II)，然后将其环化为甲基L-3-(N-苄氧羰基-L-丙氨酰)-2-氧代-恶唑烷-4-羧酸酯 (III) 与 N-苄氧羰基-L-丙氨酰-3-氯-L-丙氨酸甲酯 (IV) 在二甲苯中回流。通过 III 的温和碱性水解，N-苄氧羰基-L-丙氨酸和 L-2-氧代-恶唑烷-4-羧酸 (V) 由于肽键的选择性裂解而分离，其中氨基丝氨酸残基参与了。这种方法也适用于其他三种丝氨酸肽；得到了同样的结果。
• <b>Peptide Synthesis <b><i>via</i></b> Oxidative Activation of Acid Hydrazides</b>
  作者：Y. Wolman、P. M. Gallop、A. Patchornik、A. Berger

  DOI：10.1021/ja00869a024

  日期：1962.5
• Protein Backbone Modification by Novel C.alpha.-C Side-Chain Scission
  作者：Darshan Ranganathan、Narendra K. Vaish、Kavita Shah

  DOI：10.1021/ja00094a008

  日期：1994.7

  alpha-Ketoamide (-NH-CO-CO-) units in intact peptides are generated from Ser/Thr residues via Ru(VIII)catalyzed C-alpha-C side-chain scission. Facets associated with this novel cu-carbon modification have been probed with 75 peptides chosen to represent every possible peptide environment. The reactions were carried out at room temperature with in situ generated Ru(VIII) in biphasic (CH3CN/CCl4/pH 3 phosphate buffer, 1:1:2 v/v) medium. Whereas Ser/Thr residues placed at the C-terminal end in peptides undergo N-C bond scission leading to des-Ser/Thr peptide amides-thus acting as Gly equivalents in simulating the alpha-amidating action of pituitary enzymes-those located at the N-terminal or nonterminal or even at the C-terminal position (protected as amide) were found to undergo oxidative C-C bond scission (involving C-alpha and C side-chain bond), resulting in the generation of alpha-ketoamide (-NH-CO-CO-) units in the intact peptide backbone. The difference in the products arising from C-alpha-C side-chain scission of Ser/Thr esters and amides is rationalized on the basis of a common mechanism involving either oxaloesters [Pep-NH-CO-COX; X = OMe] or oxalamides [X = NH2 or NH-Pep] arising from the oxidation of initially formed carbinolamide intermediates [Pep-NH-CH(OH)-COX],wherein, while the former are shown to undergo hydrolysis to terminal amides [Pep-NH2], the oxalamides are found to be stable to hydrolysis. Ancillary noteworthy findings are those of peptide bond scission when contiguous Ser-Ser/Thr-Thr residues are present and the oxidative cleavage at C-terminal Tyr/Trp sites generating des amides. The oxidative methodology presented here is mild, simple, and practical and proceeds with chiral retention. The insensitivity of a large number of amino acid residues, such as Gly, Ala, Leu, Asn, Gln, Asp, Glu, Pro, Arg, Phe, Lys, Val, and Aib, and N-protecting groups, such as Boc, Z, and Bz, toward Ru(VIII) under the experimental conditions should make this methodology practical and useful. Sulfur-containing amino acids Cys and Met get oxidized to sulfones in the products.
• Pawelczak,K. et al., Polish Journal of Chemistry, 1979, vol. 53, p. 2003 - 2011
  作者：Pawelczak,K. et al.

  DOI：——

  日期：——