Bz-Val-NH2 | 190019-61-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: Bz-Val-NH2
• 英文别名: L-α-Benzamido-β-methylbutyramid；N-[(2S)-1-amino-3-methyl-1-oxobutan-2-yl]benzamide
• CAS: 190019-61-5
• 化学式: C₁₂H₁₆N₂O₂
• 分子量: 220.271
• InChiKey: XCZCIMFOYFLMBB-JTQLQIEISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1
• 重原子数：
  16
• 可旋转键数：
  4
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  72.2
• 氢给体数：
  2
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  Bz-Val-NH2 在 吡啶 、 盐酸 、 硫化氢 、 三氯氧磷 作用下， 以 乙醇 为溶剂， 生成 2-(1-amino-2-methyl-propyl)-thiazole-4-carboxylic acid
  参考文献：
  名称：

  660.微球菌素P的化学。第六部分 2-（1-氨基-2-甲基丙基）噻唑-4-羧酸的外消旋作用及相关研究

  摘要：

  DOI：

  10.1039/jr9610003394
• 作为产物：
  描述：

  N-benzoyl-L-valine 在 ruthenium trichloride 、 sodium periodate 、 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 以 四氯化碳 、 乙腈 为溶剂， 反应 4.5h， 生成 Bz-Val-NH2
  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

文献信息

• Stable water-soluble unit dose articles
  申请人：The Procter & Gamble Company

  公开号：EP2570474B1

  公开（公告）日：2014-11-19
• [EN] IMPROVED STRUCTURING USING AN EXTERNAL STRUCTURANT AND A COSMOTROPE<br/>[FR] STRUCTURATION AMÉLIORÉE FAISANT APPEL À UN AGENT STRUCTURANT EXTÉRIEUR ET À UN COSMOTROPE
  申请人：PROCTER & GAMBLE

  公开号：WO2014099852A1

  公开（公告）日：2014-06-26

  The structuring ability of fluid compositions comprising an amido-gellant or HEUR polymeric structurant can be improved with the addition of a cosmotrope.
• 660. Chemistry of micrococcin P. Part VI. Racemisation of 2-(l-amino-2-methylpropyl)thiazole-4-carboxylic acid, and related studies
  作者：B. M. Dean、M. P. V. Mijovi?、James Walker

  DOI：10.1039/jr9610003394

  日期：——
• 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.