ValHisPhePheCitAsnIleValThrAlaCitThrPro | 1092454-05-1

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: ValHisPhePheCitAsnIleValThrAlaCitThrPro
• 英文别名: H-Val-His-Phe-Phe-Cit-Asn-Ile-Val-Thr-Ala-Cit-Thr-Pro-OH；(2S)-1-[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-methylbutanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-5-(carbamoylamino)pentanoyl]amino]-4-oxobutanoyl]amino]-3-methylpentanoyl]amino]-3-methylbutanoyl]amino]-3-hydroxybutanoyl]amino]propanoyl]amino]-5-(carbamoylamino)pentanoyl]amino]-3-hydroxybutanoyl]pyrrolidine-2-carboxylic acid
• CAS: 1092454-05-1
• 化学式: C₇₂H₁₁₀N₂₀O₁₉
• 分子量: 1559.79
• InChiKey: JFYHZEGGUBWJMS-DJBLUWPDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.1
• 重原子数：
  111
• 可旋转键数：
  46
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.57
• 拓扑面积：
  626
• 氢给体数：
  21
• 氢受体数：
  21

反应信息

• 作为产物：
  描述：

  VHFFRNIVTARTP 在 peptidylarginine deiminases II 、 calcium chloride 、 1,4-二巯基-2,3-丁二醇 作用下， 反应 48.0h， 生成 ValHisPhePheCitAsnIleValThrAlaCitThrPro
  参考文献：
  名称：

  Citrullination of Linear and Cyclic Altered Peptide Ligands from Myelin Basic Protein (MBP₈₇₋₉₉) Epitope Elicits a Th1 Polarized Response by T Cells Isolated from Multiple Sclerosis Patients: Implications in Triggering Disease

  摘要：

  Derangement of cellular immunity is central in the pathophysiology of multiple sclerosis (MS) and is often manifested by abnormal cytokine production. We investigated cytokine secretion in peripheral blood mononuclear cells (PBMC) of 18 MS patients and 15 controls and correlated cytokine polarization with the nature of antiorenic stimulus. We synthesized two novel citrullinated peptides, linear [Cit(91), Ala(96), Cit(97)]MBP87-99 and cyclo(87-99)[Cit(91), Ala(96), Cit(97)]MBP87-99 that resulted from citrullination of 91,97 Arg residues in antagonists, linear [Arg(91), Ala(96)]MBP87-99 and cyclo(87-99)[Arg(91), Ala(96)] MBP87-99 peptides. PBMC from MS patients and controls were Cultured with citrullinated peptides, and both peptides caused a Th1 polarization in all MS patients studied. In contrast, culture with noncitrullinated MBP peptides resulted in heterogeneous cytokine secretion that differed between individual patients. Thus, citrullination of self-antigens may potentially trigger disease in susceptible individuals. This finding may open new avenues in drug design of new substances that inhibit citrullination and arrest epitope spreading and worsening of MS.

  DOI：

  10.1021/jm800891n