xenopsin | 117442-29-2

• 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
• 英文名称: xenopsin
• 英文别名: FHPKRPWIL；H-Phe-His-Pro-Lys-Arg-Pro-Trp-Ile-Leu-OH；(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-6-amino-2-[[(2S)-1-[(2S)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]pyrrolidine-2-carbonyl]amino]hexanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-3-methylpentanoyl]amino]-4-methylpentanoic acid
• CAS: 117442-29-2
• 化学式: C₆₀H₈₈N₁₆O₁₀
• 分子量: 1193.46
• InChiKey: WRKGJJMTAAGKOY-NAURNBLQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.1
• 重原子数：
  86
• 可旋转键数：
  33
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  413
• 氢给体数：
  13
• 氢受体数：
  14

反应信息

• 作为反应物：
  描述：

  xenopsin 、 O-甲基异脲 半硫酸盐 在 ammonium hydroxide 作用下， 以 水 为溶剂， 反应 1.0h， 生成
  参考文献：
  名称：

  Guanidination of lysine residue improves the sensitivity and facilitates the interpretation of free radical initiated peptide sequencing (FRIPS) mass spectrometry results

  摘要：

  Lysine-containing peptides, which are often found in tryptic peptide mixtures, frequently undergo double conjugations with o-TEMPO-Bz-C(O)- groups in TEMPO-assisted free radical-initiated peptide sequencing (FRIPS) mass spectrometry applications because of the facile conjugation reaction at the epsilon-primary amino group of the lysine side chain. Doubly conjugated peptides required an additional collisional activation step because they include two free radical initiators, which is not favorable for the applications of the FRIPS approach in practical peptide MS analysis. To avoid this issue, this study introduces a new strategy of guanidinating lysine-containing peptides prior to the o-TEMPO-Bz-C(O)- conjugation. The guanidination step was found to be readily incorporated into our TEMPO-assisted FRIPS procedure with high yield. More importantly, the guanidinated peptides were demonstrated to undergo radical-driven peptide backbone fragmentations, similar to peptides that lack a lysine residue. In summary, combined with the guanidination step, the TEMPO-assisted FRIPS MS offers another practical tool that can be used to analyze and characterize peptides. (C) 2015 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.ijms.2015.06.019

文献信息

• Guanidination of lysine residue improves the sensitivity and facilitates the interpretation of free radical initiated peptide sequencing (FRIPS) mass spectrometry results
  作者：Aeran Jeon、Song Hwangbo、E Seul Ryu、Jihye Lee、Ki Na Yun、Jin Young Kim、Bongjin Moon、Han Bin Oh

  DOI：10.1016/j.ijms.2015.06.019

  日期：2015.11

  Lysine-containing peptides, which are often found in tryptic peptide mixtures, frequently undergo double conjugations with o-TEMPO-Bz-C(O)- groups in TEMPO-assisted free radical-initiated peptide sequencing (FRIPS) mass spectrometry applications because of the facile conjugation reaction at the epsilon-primary amino group of the lysine side chain. Doubly conjugated peptides required an additional collisional activation step because they include two free radical initiators, which is not favorable for the applications of the FRIPS approach in practical peptide MS analysis. To avoid this issue, this study introduces a new strategy of guanidinating lysine-containing peptides prior to the o-TEMPO-Bz-C(O)- conjugation. The guanidination step was found to be readily incorporated into our TEMPO-assisted FRIPS procedure with high yield. More importantly, the guanidinated peptides were demonstrated to undergo radical-driven peptide backbone fragmentations, similar to peptides that lack a lysine residue. In summary, combined with the guanidination step, the TEMPO-assisted FRIPS MS offers another practical tool that can be used to analyze and characterize peptides. (C) 2015 Elsevier B.V. All rights reserved.