CAGRGDS | 1175039-16-3

• 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: CAGRGDS
• CAS: 1175039-16-3
• 化学式: C₂₃H₄₀N₁₀O₁₁S
• 分子量: 664.697
• InChiKey: SJXDBJXNLHPJEK-PEDHHIEDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.75
• 重原子数：
  45.0
• 可旋转键数：
  21.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.61
• 拓扑面积：
  357.35
• 氢给体数：
  14.0
• 氢受体数：
  12.0

反应信息

• 作为反应物：
  描述：

  3-allylamino-4-phenoxy-3-cyclobutene-1,2-dione 、 CAGRGDS 在 5,5'-二硫双(2-硝基苯甲酸) 作用下， 以 二甲基亚砜 为溶剂， 生成
  参考文献：
  名称：

  Selective Immobilization of Peptides Exclusively via N-Terminus Cysteines by Water-Driven Reactions on Surfaces

  摘要：

  Immobilizing peptides or proteins on bioinert surfaces enables the elucidation of ligand-receptor interaction in complex biological systems. Here, we report a highly chemoselective surface reaction that immobilizes peptides exclusively via N-terminus cysteine residue in a peptide. At pH 5.5, only N-terminus cysteines of peptides couple covalently with phenoxy amino squarate moieties presented oil self-assembled monolayers (SAMs) of alkailethiols oil gold Films. The selectivity of this surface reaction can tolerate the presence of internal cysteines in close proximity to basic residues such as histidines. We demonstrated this selective surface reaction by mammalian cell adhesion and by SAMDI mass spectroscopy of the SAMs.

  DOI：

  10.1021/jo901085u

文献信息

• Water-driven ligations using cyclic aminosquarates: a class of useful S_N1-like reactions
  作者：Dawei Cui、Deepali Prashar、Preeti Sejwal、Yan-Yeung Luk

  DOI：10.1039/c0cc03989f

  日期：——

  We report a class of water-soluble and -stable cyclic amino squarates that ligate with cysteine or lysine residues without side-products in an entirely aqueous environment. The ligations include addition–elimination reactions that are promoted by water in a way similar to SN1 reactions. The structural versatility of the reactants allows the potential recognition of selected amino acid residues on proteins.

  我们报道了一类水溶性和水稳定的环状氨基方形酸，它们在完全水相环境中与半胱氨酸或赖氨酸残基结合而不产生副产物。这些结合反应包括加成–消除反应，水以类似SN1反应的方式促进这些反应。反应物的结构多样性使其有潜力识别蛋白质上的特定氨基酸残基。