N-苄氧羰基丝氨酰亮氨酰胺 | 17331-87-2

• 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
• 中文名称: N-苄氧羰基丝氨酰亮氨酰胺
• 英文名称: Z-L-Ser-L-Leu-NH2
• 英文别名: N-Benzyloxycarbonylserylleucinamide；benzyl N-[(2S)-1-[[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]carbamate
• CAS: 17331-87-2
• 化学式: C₁₇H₂₅N₃O₅
• 分子量: 351.403
• InChiKey: OPXHXTSKUSVXIO-KBPBESRZSA-N

物化性质

• 熔点：
  181-183 °C(Solv: water (7732-18-5); ethanol (64-17-5))
• 沸点：
  656.9±55.0 °C(Predicted)
• 密度：
  1.218±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  25
• 可旋转键数：
  10
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  131
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  N-苄氧羰基丝氨酰亮氨酰胺 在 ruthenium trichloride 、 sodium periodate 作用下， 以 四氯化碳 、 乙腈 为溶剂， 反应 1.5h， 以80%的产率得到Z-NH-CO-CO-Leu-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
• 作为产物：
  描述：

  N-苄氧羰基-L-丝氨酸 在 α-chymotrypsin immobilised on Celite 、 Tris buffer 、 caesium carbonate 、 三乙胺 作用下， 以 甲醇 、 乙腈 为溶剂， 反应 48.0h， 生成 N-苄氧羰基丝氨酰亮氨酰胺
  参考文献：
  名称：

  在动态控制的肽合成中，通过使用氨基甲酰基甲酯作为酰基供体，扩大了α-胰凝乳蛋白酶的底物耐受性

  摘要：

  在动力学控制方法中 肽 通过α-胰凝乳蛋白酶介导的合成，可通过切换蛋白酶来实现蛋白酶底物耐受性的扩大。 酰基供体从常规的甲酯到氨基甲酰基甲酯。因此，作为典型实例，通过使用固有不良的甲基酯获得极低的偶联效率。氨基酸 基质， 翼，通过使用此特殊功能得到了显着改善 酯。在其他氨基酸残基如Gly和Ser的偶联中也观察到其改善作用。羧基 成分。

  DOI：

  10.1039/b004180g

文献信息

• Kinetically Controlled Peptide Synthesis Mediated by Papain Using the Carbamoylmethyl Ester as an Acyl Donor
  作者：Toshifumi Miyazawa、Takao Horimoto、Kayoko Tanaka

  DOI：10.1007/s10989-014-9393-0

  日期：2014.9

  carbamoylmethyl (Cam) esters as acyl donors in the presence of a cysteine protease, papain, immobilized on Celite. Several segment condensations were also achieved generally in high yields without danger of racemization and formation of the secondary-hydrolysis product. Moreover, partial sequences of some bioactive peptides were prepared through segment condensations, and aimed-at peptides were obtained generally

  在固定于硅藻土的半胱氨酸蛋白酶木瓜蛋白酶存在下，通常以高收率合成一系列二肽，其中氨基甲酰基甲基（Cam）酯为酰基供体。通常也以高收率获得数个段的缩合，而没有消旋化和形成二次水解产物的危险。此外，一些生物活性肽的部分序列是通过片段缩合制备的，并且通常以高收率获得了针对性的肽，而没有羧基组分的C-末端残基的外消旋化。因此，在半胱氨酸介导的偶联中再次确定了Cam酯在动力学控制的肽合成中的优越性。 如先前报道的被丝氨酸蛋白酶催化的那些。
• Remarkable effects of donor esters on the α-chymotrypsin-catalyzed couplings of inherently poor amino acid substrates
  作者：Toshifumi Miyazawa、Kayoko Tanaka、Eiichi Ensatsu、Ryoji Yanagihara、Takashi Yamada

  DOI：10.1016/s0040-4039(97)10798-5

  日期：1998.2

  The extremely low efficiency during the α-chymotrypsin-catalyzed coupling of an inherently poor amino acid substrate, e.g., alanine, using the methyl ester as an acyl donor was significantly improved using esters such as the 2,2,2-trifluoroethyl or carbamoylmethyl ester. The ameliorating effect of the latter ester was especially significant.

  使用酯类（例如2,2,2-三氟乙基或氨基甲酰基甲基酯）可显着改善α-胰凝乳蛋白酶催化的固有不良氨基酸底物（如丙氨酸）在使用甲基酯作为酰基供体时的极低效率。后一种酯的改善作用特别显着。
• Cross-Linked Crystals of Subtilisin:  Versatile Catalyst for Organic Synthesis
  作者：Yi-Fong Wang、Kirill Yakovlevsky、Bailing Zhang、Alexey L. Margolin

  DOI：10.1021/jo9618334

  日期：1997.5.1

  Cross-linked enzyme crystals (CLECs) of subtilisin exhibit excellent activity in aqueous and various organic solvents. This catalyst is more stable than the native enzyme in both aqueous and mixed aqueous/organic solutions. Subtilisin-CLEC was shown to be a versatile catalyst. It was used for the syntheses of peptides and peptidomimetics, mild hydrolysis of amino acid and peptide amides, enantio- and regioselective reactions, and transesterifications.
• Insulin Peptides. I. Synthesis of Cysteine-Containing Peptides Related to the A-Chain of Sheep Insulin
  作者：Panayotis G. Katsoyannis

  DOI：10.1021/ja01480a024

  日期：1961.10
• Patchornik,A. et al., Israel Journal of Chemistry, 1969, vol. 7, p. 559 - 565
  作者：Patchornik,A. et al.

  DOI：——

  日期：——