Boc-Met-OFm

• 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: Boc-Met-OFm
• 英文别名: Boc-MetOFm；9H-fluoren-9-ylmethyl (2S)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-4-methylsulfanylbutanoate
• 化学式: C₂₄H₂₉NO₄S
• 分子量: 427.565
• InChiKey: BRNPEVZBFSELBV-NRFANRHFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.99
• 重原子数：
  30.0
• 可旋转键数：
  7.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  64.63
• 氢给体数：
  1.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  Boc-Met-OFm 在 盐酸 作用下， 以 1,4-二氧六环 为溶剂， 反应 1.0h， 以95%的产率得到H-Met-OFm
  参考文献：
  名称：

  Practical Ring-Opening Strategy for the Sequence Determination of Cyclic Peptides from One-Bead-One-Compound Libraries

  摘要：

  The use of cyclic peptides in one-bead-one-compound libraries is limited by difficulties in sequencing hit compounds. Lacking a free N-terminal amine, such peptides cannot be sequenced by the Edman degradation approach, and complex fragmentation patterns are obtained by tandem mass spectrometry. To overcome this problem, we designed an alternative approach introducing a methionine residue within the macrocycle and as a linker to allow simultaneous ring-opening and release from the resin upon treatment with cyanogen bromide. The methionine linker was inverted relative to the peptide chain to allow the synthesis of cyclic peptides anchored by a lysine side chain and to avoid the presence of two C-terminal homoserine lactones on the released linear peptides. After MALDI-TOF MS/MS analysis, the peptides released from a single bead were sequenced manually and with a de novo sequencing software. The strategy described herein is compatible with commonly used amino acids and allows sequencing of cyclic peptides in one-bead-one-compound libraries, thus reducing the need for encoding.

  DOI：

  10.1021/co4000979
• 作为产物：
  描述：

  Boc-L-蛋氨酸 、 9-芴甲醇 在 4-二甲氨基吡啶 、 N,N'-二环己基碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 以74%的产率得到Boc-Met-OFm
  参考文献：
  名称：

  Practical Ring-Opening Strategy for the Sequence Determination of Cyclic Peptides from One-Bead-One-Compound Libraries

  摘要：

  The use of cyclic peptides in one-bead-one-compound libraries is limited by difficulties in sequencing hit compounds. Lacking a free N-terminal amine, such peptides cannot be sequenced by the Edman degradation approach, and complex fragmentation patterns are obtained by tandem mass spectrometry. To overcome this problem, we designed an alternative approach introducing a methionine residue within the macrocycle and as a linker to allow simultaneous ring-opening and release from the resin upon treatment with cyanogen bromide. The methionine linker was inverted relative to the peptide chain to allow the synthesis of cyclic peptides anchored by a lysine side chain and to avoid the presence of two C-terminal homoserine lactones on the released linear peptides. After MALDI-TOF MS/MS analysis, the peptides released from a single bead were sequenced manually and with a de novo sequencing software. The strategy described herein is compatible with commonly used amino acids and allows sequencing of cyclic peptides in one-bead-one-compound libraries, thus reducing the need for encoding.

  DOI：

  10.1021/co4000979

文献信息

• Practical Ring-Opening Strategy for the Sequence Determination of Cyclic Peptides from One-Bead-One-Compound Libraries
  作者：Xinxia Liang、Anick Girard、Eric Biron

  DOI：10.1021/co4000979

  日期：2013.10.14

  The use of cyclic peptides in one-bead-one-compound libraries is limited by difficulties in sequencing hit compounds. Lacking a free N-terminal amine, such peptides cannot be sequenced by the Edman degradation approach, and complex fragmentation patterns are obtained by tandem mass spectrometry. To overcome this problem, we designed an alternative approach introducing a methionine residue within the macrocycle and as a linker to allow simultaneous ring-opening and release from the resin upon treatment with cyanogen bromide. The methionine linker was inverted relative to the peptide chain to allow the synthesis of cyclic peptides anchored by a lysine side chain and to avoid the presence of two C-terminal homoserine lactones on the released linear peptides. After MALDI-TOF MS/MS analysis, the peptides released from a single bead were sequenced manually and with a de novo sequencing software. The strategy described herein is compatible with commonly used amino acids and allows sequencing of cyclic peptides in one-bead-one-compound libraries, thus reducing the need for encoding.