α-conotoxin S I | 133605-58-0

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: α-conotoxin S I
• 英文别名: H-Ile-Cys(1)-Cys(2)-Asn-Pro-Ala-Cys(1)-Gly-Pro-Lys-Tyr-Ser-Cys(2)-NH2；(1R,10S,13S,16S,19S,22R,27R,30S,36S,39S,46R)-13-(4-aminobutyl)-46-[[(2S,3S)-2-amino-3-methylpentanoyl]amino]-30-(2-amino-2-oxoethyl)-19-(hydroxymethyl)-16-[(4-hydroxyphenyl)methyl]-39-methyl-2,5,11,14,17,20,28,31,37,40,47-undecaoxo-24,25,43,44-tetrathia-3,6,12,15,18,21,29,32,38,41,48-undecazatetracyclo[25.14.7.06,10.032,36]octatetracontane-22-carboxamide
• CAS: 133605-58-0
• 化学式: C₅₅H₈₄N₁₆O₁₆S₄
• 分子量: 1353.63
• InChiKey: UMSRVAZBHUJACA-UOSOHNMVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.5
• 重原子数：
  91
• 可旋转键数：
  14
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  612
• 氢给体数：
  16
• 氢受体数：
  22

反应信息

• 作为产物：
  描述：

  alpha-conotoxin SI (reduced) 在 L-半胱氨酸 、 L-胱氨酸 作用下， 以 乙腈 为溶剂， 反应 48.0h， 生成 α-conotoxin S I
  参考文献：
  名称：

  High-throughput production of two disulphide-bridge toxins

  摘要：

  使用36种属于两个二硫键毒素的四个不同家族的毒素，开发了一种快速高效的生产方法，与高通量筛选兼容。最终的毒素通过HPLC共沉淀、CD和药理学研究进行了表征。

  DOI：

  10.1039/c4cc02679a

文献信息

• N-Methyl-phenacyloxycarbamidomethyl (Pocam) group: a novel thiol protecting group for solid-phase peptide synthesis and peptide condensation reactions
  作者：Hidekazu Katayama、Yoshiaki Nakahara、Hironobu Hojo

  DOI：10.1039/c1ob05253e

  日期：——

  In the so-called thioester method for the condensation of peptide segments, protecting groups for amino and thiol groups are required for chemoselective ligation. In this study, we developed a novel thiol protecting group, N-methyl-phenacyloxycarbamidomethyl (Pocam). We used it for protection of cysteine side chains, and synthesized Pocam-containing peptides and peptide thioesters. These were condensed

  在用于肽段的缩合的所谓硫酯方法中，化学选择性连接需要氨基和硫醇基的保护基。在这项研究中，我们开发了一种新型的硫醇保护基团，即N-甲基-苯甲酰氧基氨基甲酰氨基甲基（Pocam）。我们将其用于保护半胱氨酸侧链，并合成了含有Pocam的肽和肽硫酯。通过硫酯法将它们冷凝。缩合反应后，通过Zn / AcOH处理裂解Pocam基团。同时，用于保护赖氨酸侧链的叠氮基也被转化为氨基，表明该保护基策略将肽缩合反应后的去保护反应简化为仅一步。
• N-chlorosuccinimide, an efficient peptide disulfide bond-forming reagent in aqueous solution
  作者：Tobias M. Postma、Fernando Albericio

  DOI：10.1039/c3ra43149e

  日期：——

  A novel method has been developed for the efficient formation of peptide disulfide bonds under aqueous conditions using N-chlorosuccinimide. Complete disulfide bond formation is achieved in 15 min with solvent mixtures containing water and acetonitrile.

  利用 N-氯代丁二酰亚胺开发了一种在水性条件下高效形成肽二硫键的新方法。在含有水和乙腈的混合溶剂中，15 分钟内就能完全形成二硫键。
• N-Halosuccinimides mediated deprotection of cysteine-S protecting groups for one-pot regioselective synthesis of disulfide bonds in peptides under mild aqueous conditions
  作者：Yueyue Xing、Yafang Wang、Dongying Ma、Shigang Shen、Changying Song、Nan Zhang、Tianyu Bo、Tiesheng Shi、Shuying Huo

  DOI：10.1016/j.tetlet.2023.154459

  日期：2023.3

  deprotect these protecting groups to directly form an intramolecular disulfide bond in peptide. In addition, all the deprotection reactions were complete within 10 min, conferring fast reaction rates. Moreover, formation of a hydrolytic stable halosulfonium cation was revealed to play a critical role in these deprotection reactions. When NCS and NBS were employed for deprotecting these groups, two disulfide

  侧链受乙酰氨基甲基 (Acm)、1,3-噻唑烷-4-羰基 (Thz) 和叔丁基 ( t Bu)保护的半胱氨酸 (Cys) 通常用于合成肽中正确的二硫键。这些保护基团的脱保护可以通过在苛刻的去除条件下使用金属盐来实现。在这项工作中，N-氯代琥珀酰亚胺 (NCS) 和N-溴代琥珀酰亚胺 (NBS) 被证明可以使这些保护基脱保护，从而直接在肽中形成分子内二硫键。此外，所有脱保护反应都在 10 分钟内完成，反应速度很快。此外，水解稳定的卤代硫阳离子的形成被发现在这些脱保护反应中起着关键作用。当使用NCS和NBS对这些基团进行脱保护时，通过一锅法区域选择性合成了α-芋螺毒素SI、α-芋螺毒素IMI和apamin中的两个二硫键，获得了令人满意的收率。
• Detection of Thiol Functionality and Disulfide Bond Formation by Polyoxometalate
  作者：Hiroyuki Konno、Haruto Yasumiishi、Reika Aoki、Ikumi Nitanai、Shigekazu Yano

  DOI：10.1021/acscombsci.0c00176

  日期：2020.12.14

  The detection of thiol functionality and intramolecular disulfide bond formation of peptides using the α-Keggin type polyoxometalate molybdenum-oxygen cluster (H3PMo12O40·nH2O) is described. Our method entails the addition of this polyoxometalate to solutions of thiol, whereupon the color of the solution changes from colorless to deep blue. Reduction of the polyoxometalate from Mo(VI) to Mo(V) occurs with concomitant oxidation of the thiol functionality, to form disulfide bonds. To exemplify the utility this phenomenon, we accomplished the oxidation of glutathione, reduced linear oxytocin, bactenecin, and α-conotoxin SI; all of which proceeded smoothly and in good conversion in 24 h to less and were accomplished by a change in the color of the reaction solutions.