temporin B | 188713-70-4

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: temporin B
• 英文别名: LLPIVGNLLKSLL-NH2；(2S)-N-[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-1-oxohexan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]-2-[[2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-amino-4-methylpentanoyl]amino]-4-methylpentanoyl]pyrrolidine-2-carbonyl]amino]-3-methylpentanoyl]amino]-3-methylbutanoyl]amino]acetyl]amino]butanediamide
• CAS: 188713-70-4
• 化学式: C₆₇H₁₂₂N₁₆O₁₅
• 分子量: 1391.8
• InChiKey: AYROABJJLVQQJK-UCGIAFIRSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  98
• 可旋转键数：
  46
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.79
• 拓扑面积：
  499
• 氢给体数：
  16
• 氢受体数：
  17

反应信息

• 作为产物：
  描述：

  Fmoc-甘氨酸 、 Fmoc-L-缬氨酸 、 Fmoc-L-亮氨酸 、 Fmoc-L-脯氨酸 、 FMOC-O-叔丁基-L-丝氨酸 、 Fmoc-L-异亮氨酸 、 N-alpha-芴甲氧羰基-N-epsilon-叔丁氧羰基-L-赖氨酸 、 Fmoc-N-三苯甲基-L-天冬酰胺 在 N-甲基吗啉 、 1-羟基苯并三唑 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 哌啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 0.84h， 生成 temporin B
  参考文献：
  名称：

  Design, structural and functional characterization of a Temporin-1b analog active against Gram-negative bacteria

  摘要：

  Background: Temporins are small antimicrobial peptides secreted by the Rana temporaria showing mainly activity against Gram-positive bacteria. However, different members of the temporin family, such as Temporin B, act in synergy also against Gram-negative bacteria. With the aim to develop a peptide with a wide spectrum of antimicrobial activity we designed and analyzed a series of Temporin B analogs.Methods: Peptides were initially obtained by Ala scanning on Temporin B sequence; antimicrobial activity tests allowed to identify the TB_G6A sequence, which was further optimized by increasing the peptide positive charge (TB_KKG6A). Interactions of this active peptide with the LPS of E. coli were investigated by CD, fluorescence and NMR.Results: TB_KKG6A is active against Gram-positive and Gram-negative bacteria at low concentrations. The peptide strongly interacts with the LPS of Gram-negative bacteria and folds upon interaction into a kinked helix.Conclusion: Our results show that it is possible to widen the activity spectrum of an antimicrobial peptide by subtle changes of the primary structure. TB_KKG6A, having a simple composition, a broad spectrum of antimicrobial activity and a very low hemolytic activity, is a promising candidate for the design of novel antimicrobial peptides.General significance: The activity of antimicrobial peptides is strongly related to the ability of the peptide to interact and break the bacterial membrane. Our studies on TB_KKG6A indicate that efficient interactions with LPS can be achieved when the peptide is not perfectly amphipathic, since this feature seems to help the toroidal pore formation process. (C) 2013 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.bbagen.2013.01.026

文献信息

• Studies on the antileishmanial properties of the antimicrobial peptides temporin A, B and 1Sa
  作者：Frances L. Chadbourne、Catriona Raleigh、Hayder Z. Ali、Paul W. Denny、Steven L. Cobb

  DOI：10.1002/psc.1398

  日期：2011.11

  of these AMPs against L. mexicana amastigotes was low. This suggests that amastigotes from different Leishmania species display varying susceptibility to peptides from the temporin family, perhaps indicating differences in their surface structure, the proposed target of these AMPs. In contrast, insect stage L. mexicana promastigotes were sensitive to two of the screened temporins which clearly demonstrates

  鉴于利什曼病可用药物的缺乏和毒性，再加上耐药性的出现，发现这种被忽视的热带疾病的新疗法被认为是当务之急。因此，抗菌肽 (AMPs) 已被提议作为对抗致病利什曼原虫、昆虫媒介传播的原生动物寄生虫的有前景的化合物。在这里，AMP temporins A、B 和 1Sa 已被合成并筛选出对抗Leishmania mexicana昆虫阶段前鞭毛体和哺乳动物阶段无鞭毛体的活性，这是人类皮肤病的重要原因。与之前对其他物种的研究相比，这些 AMP 对L. mexicana的活性无鞭毛体低。这表明来自不同利什曼原虫物种的无鞭毛体对 temporin 家族的肽表现出不同的敏感性，这可能表明它们的表面结构存在差异，这些 AMP 的拟议目标。相比之下，昆虫阶段L. mexicana promastigotes 对两种筛选的 temporins 敏感，这清楚地证明了针对两种形式的寄生虫筛选 AMP 的重要性。版权所有
• Design, structural and functional characterization of a Temporin-1b analog active against Gram-negative bacteria
  作者：Concetta Avitabile、Fortuna Netti、Giuseppina Orefice、Maddalena Palmieri、Nunzia Nocerino、Gaetano Malgieri、Luca D. D'Andrea、Rosanna Capparelli、Roberto Fattorusso、Alessandra Romanelli

  DOI：10.1016/j.bbagen.2013.01.026

  日期：2013.6

  Background: Temporins are small antimicrobial peptides secreted by the Rana temporaria showing mainly activity against Gram-positive bacteria. However, different members of the temporin family, such as Temporin B, act in synergy also against Gram-negative bacteria. With the aim to develop a peptide with a wide spectrum of antimicrobial activity we designed and analyzed a series of Temporin B analogs.Methods: Peptides were initially obtained by Ala scanning on Temporin B sequence; antimicrobial activity tests allowed to identify the TB_G6A sequence, which was further optimized by increasing the peptide positive charge (TB_KKG6A). Interactions of this active peptide with the LPS of E. coli were investigated by CD, fluorescence and NMR.Results: TB_KKG6A is active against Gram-positive and Gram-negative bacteria at low concentrations. The peptide strongly interacts with the LPS of Gram-negative bacteria and folds upon interaction into a kinked helix.Conclusion: Our results show that it is possible to widen the activity spectrum of an antimicrobial peptide by subtle changes of the primary structure. TB_KKG6A, having a simple composition, a broad spectrum of antimicrobial activity and a very low hemolytic activity, is a promising candidate for the design of novel antimicrobial peptides.General significance: The activity of antimicrobial peptides is strongly related to the ability of the peptide to interact and break the bacterial membrane. Our studies on TB_KKG6A indicate that efficient interactions with LPS can be achieved when the peptide is not perfectly amphipathic, since this feature seems to help the toroidal pore formation process. (C) 2013 Elsevier B.V. All rights reserved.