FQNALLVR | 357943-71-6

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: FQNALLVR
• CAS: 357943-71-6
• 化学式: C₄₄H₇₃N₁₃O₁₁
• 分子量: 960.144
• InChiKey: YSFPKDZACVVOLP-ASLCGPDHSA-N

物化性质

• 密度：
  1.38±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -2.79
• 重原子数：
  68.0
• 可旋转键数：
  31.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.61
• 拓扑面积：
  415.1
• 氢给体数：
  14.0
• 氢受体数：
  12.0

反应信息

• 作为产物：
  描述：

  human serum albumin 在 trypsin 作用下， 以 aq. buffer 为溶剂， 反应 12.0h， 生成 FQNALLVR 、 LVNEVTEFAK 、 HPDYSVVLLLR 、 AFKAWAVAR 、 RHPDYSVVLLLR 、 LSQRFPK 、 DVFLGMFLYEYAR(1Met-ox) 、 RHPYFYAPELLFFAK 、 YLYEIAR
  参考文献：
  名称：

  Glycated Human Serum Albumin Isolated from Poorly Controlled Diabetic Patients Impairs Cholesterol Efflux from Macrophages: An Investigation by Mass Spectrometry

  摘要：

  高级糖基化终产物通过引发炎症、产生反应性氧化物和内质网（ER）应激，损害ABCA-1介导的胆固醇外流。利用基质辅助激光解吸/电离（MALDI）质谱法测定了1型和2型糖尿病患者人血清白蛋白（HSA）的糖基化水平，并将其与ER功能和细胞胆固醇外流受损的可能性相关联。将健康人和糖尿病患者的MALDI谱进行比较，发现1型糖尿病患者的HSA平均质量增加了1297 Da，2型糖尿病患者的HSA平均质量增加了890 Da。这些值反映了至少8个葡萄糖单元和5个葡萄糖单元的平均凝聚。将小鼠腹腔巨噬细胞用来测量Grp78、Grp94、蛋白质二硫键异构酶（PDI）、钙调蛋白（CRT）和ABCA-1的表达，分别用来处理来自对照组、1型和2型糖尿病患者的HSA。使用HSA来处理过载14C-胆固醇的J774巨噬细胞，并进一步与apo A-1孵育以确定胆固醇外流。在细胞功能试验中进行了包括1型和2型糖尿病患者的HSA的综合分析。在巨噬细胞中，与来自对照组的HSA相比，PDI表达增加了89%，CRT增加了3.4倍。与来自对照组的HSA相比，暴露于1型和2型糖尿病患者的HSA的巨噬细胞中，ABCA-1蛋白水平和apo A-I介导的胆固醇外流分别降低了50%和60%。我们提供证据表明，体内白蛋白中发生的糖基化水平损害了与巨噬细胞反向胆固醇转运受损有关的ER功能，从而促进了糖尿病的动脉粥样硬化。

  DOI：

  10.1255/ejms.1322

文献信息

• Advantages of pyrene derivatization to site-specific glycosylation analysis on MALDI mass spectrometry
  作者：Takashi Nishikaze、Hisako Okumura、Hiroshi Jinmei、Junko Amano

  DOI：10.1016/j.ijms.2012.08.006

  日期：2013.1

  Glycoproteomics involving the analysis of glycopeptides by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is a new and attractive technique. However, quantitative performance in MALDI-MS is hampered by its poor reproducibility among laser shots. 2,5-Dihydroxybenzoic acid (DHBA) is a useful matrix for glycopeptides but forms highly heterogeneous crystals. In this study, we have investigated the distribution of significant signals generated from a sample of glycopeptides on the target plate using a MALDI imaging technique. MALDI images of glycopeptides, which have different glycans on the same peptide, in the Lys-C digests of bovine ribonuclease B were identical. Thus, all glycoforms on a given peptide can be detected at the same laser irradiation spot simultaneously, which offers a significant advantage over other techniques. A similar result was observed with glycopeptides of human serum immunoglobulin G. Interestingly, distinct MALDI images were observed for glycopeptides having different amino acid sequences, despite having an identical glycan structure. The common peptides, which were glycosylated or non-glycosylated, or sialylated or desialylated gave similar MALDI images. Taken together, our results suggest that sweet spot localization of glycopeptides is dependent on the peptide moiety rather than the glycan structure. Furthermore, introduction of pyrene group to glycopeptides which have different peptides result in a uniform MALDI image. It suggested that pyrene derivatization in MALDI-MS facilitates straightforward analysis of a glycopeptide mixture because the same mass spectrum can be obtained at every sweet spot in addition to increase in signal intensity. Thus, this study validates the use of MALDI-MS for site-specific glycoprofiling at the glycopeptide level. (c) 2012 Published by Elsevier B.V.