| 1315619-43-2

• CAS: 1315619-43-2
• 化学式: C₈₄H₁₁₄F₇N₂₁O₂₂
• 分子量: 1902.95
• InChiKey: BHXJPITVVKIDKU-ZRPAOJIXSA-N

反应信息

• 作为产物：
  描述：

  Fmoc-Gly-Pro-Flp-OH 在 哌啶 、 N,N-二甲基甲酰胺 作用下， 生成
  参考文献：
  名称：

  Interstrand Dipole-Dipole Interactions Can Stabilize the Collagen Triple Helix

  摘要：

  The amino acid sequence of collagen is composed of GlyXaaYaa repeats. A prevailing paradigm maintains that stable collagen triple helices form when (2S)-proline (Pro) or Pro derivatives that prefer the C-gamma-endo ring pucker are in the Xaa position and Pro derivatives that prefer the C-gamma-exo ring pucker are in the Yaa position. Anomalously, an amino acid sequence in an invertebrate collagen has (2S, 4R)-4-hydroxyproline (Hyp), a C-gamma-exo-puckered Pro derivative, in the Xaa position. In certain contexts, triple helices with Hyp in the Xaa position are now known to be hyperstable. Most intriguingly, the sequence (GlyHypHyp)(n) forms a more stable triple helix than does the sequence (GlyProHyp)(n). Competing theories exist for the physicochemical basis of the hyperstability of (GlyHypHyp) n triple helices. By synthesizing and analyzing triple helices with different C-gamma-exo-puckered proline derivatives in the Xaa and Yaa positions, we conclude that interstrand dipole-dipole interactions are the primary determinant of their additional stability. These findings provide a new framework for understanding collagen stability.

  DOI：

  10.1074/jbc.m110.199984