leucyl-glycine amide trifluoroacetate | 82636-86-0

• 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: leucyl-glycine amide trifluoroacetate
• 英文别名: TFA*H-Leu-Gly-NH2；L-Leucyl-glycine amide trifluoroacetate；L-leucylglycinamide trifluoroacetate；(2S)-2-amino-N-(2-amino-2-oxoethyl)-4-methylpentanamide;2,2,2-trifluoroacetic acid
• CAS: 82636-86-0
• 化学式: C₂HF₃O₂*C₈H₁₇N₃O₂
• 分子量: 301.266
• InChiKey: BKTDHCOUKSRQRF-RGMNGODLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.41
• 重原子数：
  20
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.7
• 拓扑面积：
  136
• 氢给体数：
  4
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  leucyl-glycine amide trifluoroacetate 、 PChd-L-Pro-OH 在 N-甲基吗啉 、 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 生成 PChd-L-Pro-L-Leu-Gly-NH2
  参考文献：
  名称：

  肽与N- Phd保护基合成人淋巴母细胞干扰素疏水片段14-20 L-Ala-Leu-Ile-Leu-Leu-Ala-Gln的合成†

  摘要：

  氨基酸酯以59–97％的产率转化为N-（3,5-二叔丁基-4-氧代-1-苯基-2,5-环己二烯基）氨基酸酯（N -PChd氨基酸酯）8经由在2,6-存在阳极氧化二-叔丁基-4-苯基苯酚（1A）。水解8导致相应的N -PChd氨基酸9。新型的PChd保护基对碱性试剂稳定，可以通过氢化或酸解去除，并且对寡肽在有机溶剂中表现出良好的增溶性能。ñ-PChd氨基酸无需消旋就可以偶联，它们易于制备和存储，并且易于结晶。-使用常规的肽合成方法和在二氯甲烷中或在催化氢化中用10–50％三氟乙酸进行PChd脱保护的方法，制备了七肽HuIFN-α（Ly）14–20 L-Ala-Leu-Ile-Leu-Leu-Ala-Gln。如柱色谱和薄层色谱法，13 C-NMR光谱法，手性气相色谱法和常用分析方法所示，合成得到的收率和纯度均很高。

  DOI：

  10.1002/jlac.198219820608
• 作为产物：
  描述：

  L-亮氨酸苄基酯 在 2,6-二甲基吡啶 、 sodium hydroxide 、 N,N,N,N-tetraethylammonium tetrafluoroborate 、 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 13.25h， 生成 leucyl-glycine amide trifluoroacetate
  参考文献：
  名称：

  肽与N- Phd保护基合成人淋巴母细胞干扰素疏水片段14-20 L-Ala-Leu-Ile-Leu-Leu-Ala-Gln的合成†

  摘要：

  氨基酸酯以59–97％的产率转化为N-（3,5-二叔丁基-4-氧代-1-苯基-2,5-环己二烯基）氨基酸酯（N -PChd氨基酸酯）8经由在2,6-存在阳极氧化二-叔丁基-4-苯基苯酚（1A）。水解8导致相应的N -PChd氨基酸9。新型的PChd保护基对碱性试剂稳定，可以通过氢化或酸解去除，并且对寡肽在有机溶剂中表现出良好的增溶性能。ñ-PChd氨基酸无需消旋就可以偶联，它们易于制备和存储，并且易于结晶。-使用常规的肽合成方法和在二氯甲烷中或在催化氢化中用10–50％三氟乙酸进行PChd脱保护的方法，制备了七肽HuIFN-α（Ly）14–20 L-Ala-Leu-Ile-Leu-Leu-Ala-Gln。如柱色谱和薄层色谱法，13 C-NMR光谱法，手性气相色谱法和常用分析方法所示，合成得到的收率和纯度均很高。

  DOI：

  10.1002/jlac.198219820608

文献信息

• Enzymatically catalyzed synthesis of oxytocin fragments 1-6 and 7-9
  作者：Václav Čeřovský、Karel Jošt

  DOI：10.1135/cccc19852775

  日期：——

  Papain, α-chymotrypsin, thermolysin and elastase were utilized in the synthesis of peptide bonds of the protected oxytocin nonapeptide, except the S-benzylcysteine-proline bond. Amino groups were protected with benzyloxycarbonyl or tert-butyloxycarbonyl groups, carboxy groups as ethyl ester, phenylhydrazides or amides. The cysteine sulfhydryl group was blocked with the benzyl group whereas the tyrosine hydroxyl was unprotected. Most of the fragments were synthesized in satisfactory yields using an equimolar ratio of both reaction components and minimal (experimentally determined) amount of the given enzyme.

  木瓜酶、α-胰蛋白酶、热溶菌素和弹性蛋白酶被用于合成受保护的催产素非肽九肽的肽键，除了S-苄基半胱氨酸-脯氨酸键。氨基团被苄氧羰基或叔丁氧羰基团保护，羧基被乙酯、苯肼或酰胺保护。半胱氨酸巯基被苄基团阻断，而酪氨酸羟基未被保护。大多数片段在使用等摩尔比的反应组分和最小（经实验确定的）给定酶量的情况下以令人满意的产率合成。
• A Convenient On-Site Oxidation Strategy for the N-Hydroxylation of Melanostatin Neuropeptide Using Cope Elimination
  作者：Ivo E. Sampaio-Dias、Sara C. Silva-Reis、Beatriz L. Pires-Lima、Xavier Cruz Correia、Hugo F. Costa-Almeida

  DOI：10.1055/a-1695-1095

  日期：2022.4

  N-hydroxylation of proline residue in Melanostatin (MIF-1) neuropeptide is reported. This methodology is grounded on the incorporation of N-(cyanoethyl)prolyl residue followed by on-site oxidation by Cope elimination with m-chloroperbenzoic acid, exploring the unrecognized dual role of the cyanoethyl group as an effective N-protecting group under peptide synthesis conditions and as a suitable leaving group during

  报道了一种方便的合成方案，用于对黑素抑制素 (MIF-1) 神经肽中脯氨酸残基进行前所未有的N-羟基化。该方法基于引入N- (氰乙基)脯氨酸残基，然后通过用间氯过苯甲酸进行 Cope 消除进行现场氧化，探索了在肽合成条件下氰乙基作为有效N-保护基团的未被认识的双重作用并在化学选择性现场N-氧化过程中作为合适的离去基团。按照该协议， N-羟基-MIF-1 以 78% 的全球收率从N- (氰乙基)-中获得l-脯氨酸。这种合成方法为直接应用于神经化学和帕金森氏症研究的N-羟基化黑色素抑制素类似物开辟了一条新途径。
• Partially Modified Retro-Inverso Pseudopeptides as Non-natural Ligands for the Human Class I Histocompatibility Molecule HLA-A2
  作者：Gilles Guichard、Francine Connan、Roland Graff、Marina Ostankovitch、Sylviane Muller、Jean-Gérard Guillet、Jeannine Choppin、Jean-Paul Briand

  DOI：10.1021/jm9509511

  日期：1996.1.1

  Syntheses of a series of partially modified retro-inverso analogues of the antigenic peptide M58-66 derived from the influenza virus matrix protein are reported. The retro-inverso modification Psi(NH-CO) was obtained by replacement of two successive amino acid residues with a 2-substituted malonate derivative and gem-diaminoalkyl residue. The resulting compounds 1-8 were tested for their binding to the human histocompatibility class I molecule HLA-A2 in an assembly assay using lysates of peptide transporter-deficient cells T2. Specific peptide-dependent HLA-A2 assembly was revealed by an enzyme-linked immunosorbent assay. Significant HLA-A2 assembly was detected in the presence of analogues [gGly(58)-(S)mLeu(59)]-M58-66 (1a), [gGly(61)-(R,S)mPhe(62)]M58-66 (4), [gVal(63)-(R,S)mPhe(64)]M58-66 (6), and [gPhe(64)-(R,S)mAla(65)]M58-66 (7). The introduction of the retro-inverso modification between P2-P3, P3-P4, P5-P6, and P8-P9 (compounds 2, 3, 5, and 8, respectively) however led to a dramatic reduction in peptide binding to HLA-A2. Interestingly, compound 1a which contains modification between P1-P2 was found to be the most potent analogue, being able to retain the original HLA-A2 binding profile of the parent peptide M58-66. Taken together, these results and recent binding data obtained in the context of murine MHC class I molecule H-2K(d) suggest that the incorporation of peptide bond surrogates in MHC class I-restricted epitopes is a useful approach to design molecules having both increased stability and high MHC-binding capacity. Depending on their agonist or antagonist effects at the T-cell receptor, such non-natural MHC ligands are likely to find many applications in the development of peptide-based vaccines or as potential therapeutic agents in the treatment of allergies and autoimmune diseases.