L-组氨酰-L-丝氨酸 | 21438-60-8

• 物质功能分类: 生物化工 - 生化试剂 - 氨基酸
• 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: L-组氨酰-L-丝氨酸
• 中文别名: (S)-2-((S)-2-氨基-3-(1H-咪唑-4-基)丙酰胺基)-3羟基丙酸
• 英文名称: 2-[[2-amino-3-(1H-imidazol-5-yl)propanoyl]amino]-3-hydroxypropanoic acid
• 英文别名: His-Ser
• CAS: 21438-60-8
• 化学式: C₉H₁₄N₄O₄
• 分子量: 242.23
• InChiKey: KRBMQYPTDYSENE-BQBZGAKWSA-N

物化性质

• 熔点：
  138-141℃
• 沸点：
  737.6±60.0 °C(Predicted)
• 密度：
  1.492±0.06 g/cm3(Predicted)
• 物理描述：
  Solid

计算性质

• 辛醇/水分配系数(LogP)：
  -3.9
• 重原子数：
  17
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  146
• 氢给体数：
  4
• 氢受体数：
  5

安全信息

• WGK Germany：
  3
• 海关编码：
  2933290090
• 危险性防范说明：
  P261,P280,P301+P312,P302+P352,P305+P351+P338
• 危险性描述：
  H302,H315,H319,H335

文献信息

• Hydrolysis of Serine-Containing Peptides at Neutral pH Promoted by [MoO₄]^2– Oxyanion
  作者：Phuong Hien Ho、Karen Stroobants、Tatjana N. Parac-Vogt

  DOI：10.1021/ic2015034

  日期：2011.12.5

  Hydrolysis of the dipeptides glycylserine (GlySer), leucylserine (LeuSer), histidylserine (HisSer), glycylalanine (GlyAla), and serylglycine (SerGly) was examined in oxomolybdate solutions by means of 1H, 13C, and 95Mo NMR spectroscopy. In the presence of a mixture of oxomolybdates, the hydrolysis of the peptide bond in GlySer proceeded under neutral pD conditions (pD = 7.0, 60 °C) with a rate constant

  通过1 H，13 C和95 Mo NMR光谱法检查了在含氧钼酸盐溶液中二肽的甘氨酰丝氨酸（GlySer），亮氨酰丝氨酸（LeuSer），组氨酸丝氨酸（HisSer），甘氨酰丙氨酸（GlyAla）和丝氨酰甘氨酸（SerGly）的水解情况。在含氧钼酸盐的混合物存在下，GlySer中肽键的水解在中性pD条件（pD = 7.0，60°C）下以k obs = 5.9×10 –6 s –1的速率常数进行。NMR光谱没有显示出顺磁性物质形成的证据，排除了Mo（VI）还原为Mo（V）的可能性，这表明肽键的裂解是纯水解的。k的pD依赖性obs呈钟形，在pD 7.0观察到最快的卵裂。速率分布图与含氧钼酸盐物种的浓度分布图的比较涉及单钼酸盐MoO 4 2–作为动力学活性复合物。使用固定量的GlySer和不断增加的MoO 4 2–在pD 7.0下进行的动力学实验可以计算催化速率常数（k 2 = 9.25×10 –6
• Chemical isotope labeling-assisted liquid chromatography-mass spectrometry enables sensitive and accurate determination of dipeptides and tripeptides in complex biological samples
  作者：Feng-Qing Huang、Yu Wang、Ji-Wen Wang、Dai Yang、Shi-Lei Wang、Yuan-Ming Fan、Raphael N. Alolga、Lian-Wen Qi

  DOI：10.1016/j.cclet.2024.109670

  日期：2024.11

  their unique features and diverse biological functions. Achieving rapid separation and accurate quantification, however, remains a challenge because of their low abundance and the co-existence of numerous structural isomers. In this study, we developed a novel approach using isotope chemical labeling for ultrasensitive determination of di/tripeptides in biological samples. We successfully synthesized a

  小肽因其独特的特性和多样化的生物学功能而受到越来越多的关注。然而，由于其丰度低且存在多种结构异构体，实现快速分离和准确定量仍然是一个挑战。在这项研究中，我们开发了一种使用同位素化学标记超灵敏测定生物样品中二肽/三肽的新方法。我们成功合成了一种新型衍生化试剂4-(2-(乙氧基亚甲基)-3-氧代丁酰胺基)-三甲基苯胺碘化物(EOTMBA)及其氘标记同位素试剂(-EOTMBA)。总共97个小肽，包括89个二肽和8个三肽，在60℃下1.5小时内可以在​​甲醇中完全衍生化。 EOTMBA 标记后，通过 LC-MS/MS 分析在 22 分钟内完成对这些二肽/三肽的分析。该方法的准确度为 86.3%–113%，定量限范围为 0.25 fmol/L 至 5 nmol/L。利用该方法，我们对取自健康个体和胆道疾病患者的 147 份血浆、49 份尿液和 46 份胆汁样本中的二肽/三肽进行了超灵敏和准确的定量。
• Hydrolytic Activity of Vanadate toward Serine-Containing Peptides Studied by Kinetic Experiments and DFT Theory
  作者：Phuong Hien Ho、Tzvetan Mihaylov、Kristine Pierloot、Tatjana N. Parac-Vogt

  DOI：10.1021/ic300761g

  日期：2012.8.20

  Hydrolysis of dipeptides glycylserine (Gly-Ser), leucylserine (Leu-Ser), histidylserine (His-Ser), glycylalanine (Gly-Ala), and serylglycine (Ser-Gly) was examined in vanadate solutions by means of H-1, C-13, and V-51 NMR spectroscopy. In the presence of a mixture of oxovanadates, the hydrolysis of the peptide bond in Gly-Ser proceeds under the physiological pH and temperature (37 degrees C, pD 7.4) with a rate constant of 8.9 x 10(-8) s(-1). NMR and EPR spectra did not show evidence for the formation of paramagnetic species, excluding the possibility of V(V) reduction to V(IV) and indicating that the cleavage of the peptide bond is purely hydrolytic. The pD dependence of k(obs) exhibits a bell-shaped profile, with the fastest hydrolysis observed at pD 7.4. Combined H-1, C-13, and V-51 NMR experiments revealed formation of three complexes between Gly-Ser and vanadate, of which only one complex, designated Complex 2, formed via coordination of amide oxygen and amino nitrogen to vanadate, is proposed to be hydrolytically active. Kinetic experiments at pD 7.4 performed by using a fixed amount of Gly-Ser and increasing amounts of Na3VO4 allowed calculation of the formation constant for the Gly-Ser/VO43- complex (K-f = 16.1 M-1). The structure of the hydrolytically active Complex 2 is suggested also on the basis of DFT calculations. The energy difference between Complex 2 and the major complex detected in the reaction mixture, Complex 1, is calculated to be 7.1 kcal/mol in favor of the latter. The analysis of the molecular properties of Gly-Ser and their change upon different modes of coordination to the vanadate pointed out that only in Complex 2 the amide carbon is suitable for attack by the hydroxyl group in the Ser side chain, which acts as an effective nucleophile. The origin of the hydrolytic activity of vanadate is most likely a combination of the polarization of amide oxygen in Gly-Ser due to the binding to vanadate, followed by the intramolecular attack of the Ser hydroxyl group.