Biotin-GG-DEVR-CHO | 1263302-69-7

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: Biotin-GG-DEVR-CHO
• CAS: 1263302-69-7
• 化学式: C₃₄H₅₅N₁₁O₁₂S
• 分子量: 841.943
• InChiKey: PWLDCPULKMVQKF-PIJGUAIGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.66
• 重原子数：
  58.0
• 可旋转键数：
  27.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.68
• 拓扑面积：
  369.3
• 氢给体数：
  13.0
• 氢受体数：
  12.0

反应信息

• 作为产物：
  描述：

  Biotin-GG-ARFK-CHO 在 三氟乙酸 作用下， 以 水 、 乙腈 为溶剂， 反应 0.5h， 生成 Biotin-GG-DEVR-CHO
  参考文献：
  名称：

  A Peptide Aldehyde Microarray for High-Throughput Profiling of Cellular Events

  摘要：

  Microarrays provide exciting opportunities in the field of large-scale proteomics. With the aim to elucidate enzymatic activity and profiles within native biological samples, we developed a microarray comprising a focused positional-scanning library of enzyme inhibitors. The library was diversified across P-1-P-4 positions, creating 270 different inhibitor sublibraries which were immobilized onto avidin slides. The peptide aldehyde-based small-molecule microarray (SMM) specifically targeted cysteine proteases, thereby enabling large-scale functional assessment of this subgroup of proteases, within fluorescently labeled samples, including pure proteins, cellular lysates, and infected samples. The arrays were shown to elicit binding fingerprints consistent with those of model proteins, specifically caspases and purified cysteine proteases from parasites (rhodesein and cruzain). When tested against lysates from apoptotic Hela and red blood cells infected with Plasmodium falciparum, clear signatures were obtained that were readily attributable to the activity of constituent proteases within these samples. Characteristic binding profiles were further able to distinguish various stages of the parasite infection in erythrocyte lysates. By converting one of our brightest microarray hits into a probe, putative protein markers were identified and pulled down from within apoptotic Hela lysates, demonstrating the potential of target validation and discovery. Taken together, these results demonstrate the utility of targeted SMMs in dissecting cellular biology in complex proteomic samples.

  DOI：

  10.1021/ja109597v