Bz-Gly-Pro-OMe

• 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: Bz-Gly-Pro-OMe
• 英文别名: methyl (2S)-1-(2-benzamidoacetyl)pyrrolidine-2-carboxylate
• 化学式: C₁₅H₁₈N₂O₄
• 分子量: 290.319
• InChiKey: XYQQPBFPXGTMHK-LBPRGKRZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  21
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.4
• 拓扑面积：
  75.7
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Bz-Gly-Pro-OMe 在 N-溴代丁二酰亚胺(NBS) 作用下， 以 二氯甲烷 为溶剂， 反应 17.0h， 生成 Bz-Gly(SCSOEt)-Pro-OMe
  参考文献：
  名称：

  Blakskjaer; Pedersen; Skrydstrup, Journal of the Chemical Society. Perkin Transactions 1 (2001), 2001, # 7, p. 910 - 915

  摘要：

  DOI：

文献信息

• Selective Side Chain Introduction onto Small Peptides Mediated by Samarium Diiodide:  A Potential Route to Peptide Libraries
  作者：Marina Ricci、Peter Blakskjær, and、Troels Skrydstrup

  DOI：10.1021/ja0024800

  日期：2000.12.1

  A mild and simple method for the selective introduction of carbinol side chains onto glycine residues in peptides is presented as a potential route for the preparation of peptide libraries. A series of di- and tripeptides, as well as one tetrapeptide, each possessing one glycine residue, were first selectively functionalized at this amino acid unit by a two-step sequence involving bromination with

  提出了一种将甲醇侧链选择性引入肽中甘氨酸残基的温和简单的方法，作为制备肽库的潜在途径。一系列二肽和三肽，以及一个四肽，每个都有一个甘氨酸残基，首先通过两步序列在这个氨基酸单元上选择性地功能化，包括用 N-溴代琥珀酰亚胺溴化，然后通过处理不稳定的物质形成硫化物。甘氨酰溴与 2-巯基吡啶。然后在烷基醛和酮的存在下，在室温下用二碘化钐还原这些修饰的肽，以 40-65% 的产率提供一系列含有丝氨酸/苏氨酸衍生物作为新功能的肽。这些反应相当有效，考虑到烯醇中间体中存在多达四个酰胺质子。这些反应的非对映选择性很低或不存在，这归因于 (a) 单一烯醇的形成...
• The specificity of Prolyl Endopeptidase from Flavobacterium meningoseptum : mapping the S′ subsites by positional scanning via acyl transfer
  作者：Frank Bordusa、Hans-Dieter Jakubke

  DOI：10.1016/s0968-0896(98)00145-x

  日期：1998.10

  The S-1'-S-3' subsite specificity of prolyl endopeptidase from Flavobacterium meningoseptum was studied by acyl transfer to libraries of amino acid amides and peptides. Whereas the S-1' and S-3' subsites influence the specificity for the amino component by approximately one order of magnitude, the S-2' subsite possesses a markedly higher specificity. Besides the high specificity for hydrophobic residues at P-1'-P-3', proline was efficiently bound by the S-2' and S-3' subsites of the enzyme. In contrast, no binding of P-1' proline-containing peptides was observed. It could be demonstrated that the specificity of the S' subsite is not restricted to L-amino acids. Effective P'-S' interactions were also found for beta- and gamma-amino acids indicating that the enzyme does not form close contacts to the backbone of P-1' and P-2' amino acid residues. (C) 1998 Elsevier Science Ltd. All rights reserved.