H-Lys-Ala-Ala-Cys(1)-Ala-Ala-Lys-Cys(1)-Leu-Trp-Arg-NH2 | 1032140-41-2

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: H-Lys-Ala-Ala-Cys(1)-Ala-Ala-Lys-Cys(1)-Leu-Trp-Arg-NH2
• 英文别名: (4R,7S,10S,13S,16R)-7-(4-aminobutyl)-N-[(2S)-1-[[(2S)-1-[[(2S)-1-amino-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]-16-[[(2S)-2-[[(2S)-2-[[(2S)-2,6-diaminohexanoyl]amino]propanoyl]amino]propanoyl]amino]-10,13-dimethyl-6,9,12,15-tetraoxo-1,2-dithia-5,8,11,14-tetrazacycloheptadecane-4-carboxamide
• CAS: 1032140-41-2
• 化学式: C₅₃H₈₈N₁₈O₁₁S₂
• 分子量: 1217.53
• InChiKey: UTGQICIPLXTYOA-HNYYSNPSSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.8
• 重原子数：
  84
• 可旋转键数：
  29
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  543
• 氢给体数：
  17
• 氢受体数：
  17

反应信息

• 作为产物：
  描述：

  H-Lys-Ala-Ala-Cys-Ala-Ala-Lys-Cys-Leu-Trp-Arg-NH2 在 二甲基亚砜 作用下， 以 phosphate buffer 为溶剂， 生成 H-Lys-Ala-Ala-Cys(1)-Ala-Ala-Lys-Cys(1)-Leu-Trp-Arg-NH2
  参考文献：
  名称：

  Design and synthesis of cyclic disulfide-bonded antibacterial peptides on the basis of the α helical domain of Tenecin 1, an insect defensin

  摘要：

  We synthesized cyclic disulfide-bonded (i, i + 4) peptides with various net positive charges (+2-+5) from linear peptides derived from the a helical domain of Tenecin 1, an insect defensin, and investigated the effect of the intradisulfide bridge (i, i + 4) on hydrophobicity, secondary structure, leakage activity and binding activity for large unilamellar vesicles, antimicrobial activity, and hemolytic activity. Intradisulfide bridge formation of the peptides resulted in the increase of amphiphilicity and hydrophobicity. Cyclic forms of the peptides did not deeply penetrate into PG/PC (1: 1, mole ratio) large unilamellar vesicles and had a decreased lipid membrane perturbation activity for PG/PC LUVs. When the peptides interacted with PG/CL (2: 1, mole ratio) LUVs, cyclic peptides with a high net positive charge (+4-+5) showed similar binding affinities and leakage activities for vesicles to those of linear forms, whereas cyclic peptides with a low net positive charge (+2-+3) exhibited lower leakage activity than their linear forms. CD spectra indicate that the intradisulfide bridge (i, i + 4) provided little conformational constraint to linear peptides in buffer solution but resulted in the decrease of alpha helicity of the peptides in lipid membrane mimic conditions. The cyclic peptide with the highest net positive charge had a similar antibacterial activity to that of the linear peptide, whereas the cyclic peptides with a low net positive charge (+3-+4) exhibited lower antibacterial activity than their linear forms. The cyclic peptides of an appropriate net charge showed more potent activities against some bacteria than those of linear forms under high salt conditions. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.01.019