[U-13C,15N]-(20-29)huamn islet amyloid polypeptide | 138285-72-0

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: [U-13C,15N]-(20-29)huamn islet amyloid polypeptide
• 英文别名: AcHN-SNNFGAILSS-CONH2
• CAS: 138285-72-0
• 化学式: C₄₅H₇₁N₁₃O₁₆
• 分子量: 1050.14
• InChiKey: KPSVPJMEYQGYFH-LEHUKPRESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -7.95
• 重原子数：
  74.0
• 可旋转键数：
  33.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  480.96
• 氢给体数：
  16.0
• 氢受体数：
  16.0

反应信息

• 作为产物：
  描述：

  Fmoc-甘氨酸 、 Fmoc-L-亮氨酸 、 Fmoc-L-丙氨酸 、 Fmoc-L-苯丙氨酸 、 FMOC-O-叔丁基-L-丝氨酸 、 乙酸酐 、 Fmoc-L-异亮氨酸 、 Fmoc-N-三苯甲基-L-天冬酰胺 在 C₁₅H₂₃N₂O₄Pol 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 、 哌啶 作用下， 以 N-甲基吡咯烷酮 、 N,N-二甲基甲酰胺 为溶剂， 反应 0.14h， 生成 [U-13C,15N]-(20-29)huamn islet amyloid polypeptide
  参考文献：
  名称：

  The Importance of Being Capped: Terminal Capping of an Amyloidogenic Peptide Affects Fibrillation Propensity and Fibril Morphology

  摘要：

  The formation of aggregated fibrillar beta-sheet structures has been proposed to be a generic feature of proteins. Aggregation propensity is highly sequence dependent, and often only part of the protein is incorporated into the fibril core. Therefore, shorter peptide fragments corresponding to the fibril core are attractive fibrillation models. The use of peptide models introduces new termini into the fibrils, yet little attention has been paid to the role these termini may play in fibrillation. Here, we report that terminal modifications of a 10-residue peptide fragment of human islet amyloid polypeptide strongly affect fibrillation kinetics and the resulting fibril morphology. Capping of the N-terminus abolishes fibrillation, while C-terminal capping results in fibrils with a twisted morphology. Peptides with either both termini free or both termini capped form flat fibrils. Molecular dynamics simulations reveal that the N-terminal acetyl cap folds up and interacts with the peptide's hydrophobic side chains, while the uncapped N-terminus in the C-terminally capped version results in twisting of the fibrils due to charge repulsion from the free N-termini. Our results highlight the role of terminal interactions in fibrillation of small peptides and provide molecular insight into the consequences of C-terminal modifications frequently found in peptide hormones in vivo.

  DOI：

  10.1021/bi500674u