Fmoc-D,L-Hcy(Trt)-OH

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: Fmoc-D,L-Hcy(Trt)-OH
• 英文别名: N-[(9H-Fluoren-9-ylmethoxy)carbonyl]triphenyl-D-methionine；2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-tritylsulfanylbutanoic acid
• 化学式: C₃₈H₃₃NO₄S
• 分子量: 599.75
• InChiKey: FKBGJLDYRSFHBT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  8.4
• 重原子数：
  44
• 可旋转键数：
  12
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.16
• 拓扑面积：
  101
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  Fmoc-D,L-Hcy(Trt)-OH 、 5-丁基吡啶-2-羧酸 、 Fmoc-D-苯丙氨酸 生成 (2R)-2-(2-(3-butylpicolinamido)-4-mercaptobutanamido)-3-phenylpropanoic acid
  参考文献：
  名称：

  Homo-cysteinyl peptide inhibitors of the L1 metallo-β-lactamase, and SAR as determined by combinatorial library synthesis

  摘要：

  Homo-cysteinyl peptides were found to be more active than cysteinyl peptides toward L1 metallo-beta-lactamase as reversible competitive inhibitors. A combinatorial library of more than 90 homo-cysteinyl peptides was synthesized and screened for their inhibitory activity toward the L1 enzyme. A systematic structure-activity relationship analysis has revealed the preferred interaction groups for Ll conserved binding sites of beta-lactam substrates. The most active compound 95b, had a K-i of 2.1 nM. (c) 2006 Published by Elsevier Ltd.

  DOI：

  10.1016/j.bmcl.2006.07.001

文献信息

• MASP INHIBITORY COMPOUNDS AND USES THEREOF
  申请人：Bayer Aktiengesellschaft

  公开号：US20210246166A1

  公开（公告）日：2021-08-12

  The present invention relates to novel Mannose-binding lectin (MBL)-associated serine protease (MASP) inhibitory compounds, as well as analogues and derivatives thereof, to processes for the preparation thereof, to the use thereof alone or in combinations for treatment and/or prevention of diseases and to the use thereof for production of medicaments for treatment and/or prevention of diseases, especially for treatment and/or prevention of renal and cardiovascular disorders and of ischemia reperfusion injuries.
• Homo-cysteinyl peptide inhibitors of the L1 metallo-β-lactamase, and SAR as determined by combinatorial library synthesis
  作者：Qin Sun、Andy Law、Michael W. Crowder、H. Mario Geysen

  DOI：10.1016/j.bmcl.2006.07.001

  日期：2006.10

  Homo-cysteinyl peptides were found to be more active than cysteinyl peptides toward L1 metallo-beta-lactamase as reversible competitive inhibitors. A combinatorial library of more than 90 homo-cysteinyl peptides was synthesized and screened for their inhibitory activity toward the L1 enzyme. A systematic structure-activity relationship analysis has revealed the preferred interaction groups for Ll conserved binding sites of beta-lactam substrates. The most active compound 95b, had a K-i of 2.1 nM. (c) 2006 Published by Elsevier Ltd.