11-[10-(4-Nitro-phenoxycarbonyl)-decyldisulfanyl]-undecanoic acid 4-nitro-phenyl ester | 858972-33-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚酯
• 英文名称: 11-[10-(4-Nitro-phenoxycarbonyl)-decyldisulfanyl]-undecanoic acid 4-nitro-phenyl ester
• 英文别名: (4-nitrophenyl) 11-[[11-(4-nitrophenoxy)-11-oxoundecyl]disulfanyl]undecanoate
• CAS: 858972-33-5
• 化学式: C₃₄H₄₈N₂O₈S₂
• 分子量: 676.896
• InChiKey: FWUBASXRGACHFO-UHFFFAOYSA-N

物化性质

• 熔点：
  58-60 °C
• 沸点：
  761.3±45.0 °C(Predicted)
• 密度：
  1.178±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  10.42
• 重原子数：
  46.0
• 可旋转键数：
  27.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  138.88
• 氢给体数：
  0.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  11-[10-(4-Nitro-phenoxycarbonyl)-decyldisulfanyl]-undecanoic acid 4-nitro-phenyl ester 、 N-Boc-1,11-二氨基-3,6,9-三氧杂十一烷 在 吡啶 、 4-二甲氨基吡啶 作用下， 反应 17.0h， 以84%的产率得到bis{10-[11-(N-tert-butoxycarbonylamino)-3,6,9-trioxaundecylcarbamoyl]undecanyl} disulfide
  参考文献：
  名称：

  Efficient one-cycle affinity selection of binding proteins or peptides specific for a small-molecule using a T7 phage display pool

  摘要：

  Here, we report an efficient one-cycle affinity selection using a natural-protein or random-peptide T7 phage pool for identification of binding proteins or peptides specific for small-molecules. The screening procedure involved a cuvette type 27-MHz quartz-crystal microbalance (QCM) apparatus with introduction of self-assembled monolayer (SAM) for a specific small-molecule immobilization on the gold electrode surface of a sensor chip. Using this apparatus, we attempted an affinity selection of proteins or peptides against synthetic ligand for FK506-binding protein (SLF) or irinotecan (Iri, CPT-11). An affinity selection using SLF-SAM and a natural-protein T7 phage pool successfully detected FK506-binding protein 12 (FKBP12)-displaying T7 phage after an interaction time of only 10 min. Extensive exploration of time-consuming wash and/or elution conditions together with several rounds of selection was not required. Furthermore, in the selection using a 15-mer random-peptide T7 phage pool and subsequent analysis utilizing receptor ligand contact (RELIC) software, a subset of SLF-selected peptides clearly pinpointed several amino-acid residues within the binding site of FKBP12. Likewise, a subset of Iri-selected peptides pinpointed part of the positive amino-acid region of residues from the Iri-binding site of the well-known direct targets, acetylcholinesterase (AChE) and carboxylesterase (CE). Our findings demonstrate the effectiveness of this method and general applicability for a wide range of small-molecules. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.09.061
• 作为产物：
  描述：

  11-巯基十一烷酸 在 吡啶 、 sodium hydroxide 、 草酰氯 、 碘 、 potassium iodide 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 24.5h， 生成 11-[10-(4-Nitro-phenoxycarbonyl)-decyldisulfanyl]-undecanoic acid 4-nitro-phenyl ester
  参考文献：
  名称：

  Immobilization of Rhodium Complexes at Thiolate Monolayers on Gold Surfaces:  Catalytic and Structural Studies

  摘要：

  Chiral rhodium-diphosphine complexes have been incorporated into self-assembled thiolate monolayers (SAMS) on gold colloids. Catalysts of this type are of interest because they combine properties of homogeneous and heterogeneous systems. In addition, it should be possible to influence the catalytic properties of the metal center by the neighboring thiolate molecules. Colloids with a diameter of ca. 3 nm, coated with a mixed monolayer of n-octanethiolates and thiolates with chiral rhodium-PYRPHOS end groups, were studied as hydrogenation catalysts. With methyl a-acetamido-cinnamate as substrate, virtually the same enantioselectivities (up to 93% ee) and full conversion were obtained as with the corresponding homogeneous [Rh(COD)(PYRPHOS)]BArF catalyst. The colloids were easily recovered by filtration and reused as catalysts three times without loss of enantioselectivity. STM studies of analogous SAMS on Au(111) gave a detailed picture of the structure and dynamics of mixed monolayers of this type. The STM images showed that the catalyst-bearing thiolates are distributed statistically on the surface and that the ordered structure of the n-octanethiolate SAM can be retained during incorporation of the catalyst-bearing thiols using the place-exchange methodology.

  DOI：

  10.1021/ja0500714

文献信息

• Identification of trimannoside-recognizing peptide sequences from a T7 phage display screen using a QCM device
  作者：Kazusa Nishiyama、Yoichi Takakusagi、Tomoe Kusayanagi、Yuki Matsumoto、Shiori Habu、Kouji Kuramochi、Fumio Sugawara、Kengo Sakaguchi、Hideyo Takahashi、Hideaki Natsugari、Susumu Kobayashi

  DOI：10.1016/j.bmc.2008.11.004

  日期：2009.1

  Here, we report on the identification of trimannoside-recognizing peptide sequences from a T7 phage display screen using a quartz-crystal microbalance (QCM) device. A trimannoside derivative that can form a self-assembled monolayer (SAM) was synthesized and used for immobilization on the gold electrode surface of a QCM sensor chip. After six sets of one-cycle affinity selection, T7 phage particles displaying PSVGLFTH (8-mer) and SVGLGLGFSTVNCF (14-mer) were found to be enriched at a rate of 17/44, 9/44, respectively, suggesting that these peptides specifically recognize trimannoside. Binding checks using the respective single T7 phage and synthetic peptide also confirmed the specific binding of these sequences to the trimannoside-SAM. Subsequent analysis revealed that these sequences correspond to part of the primary amino acid sequence found in many mannose- or hexose- related proteins. Taken together, these results demonstrate the effectiveness of our T7 phage display environment for affinity selection of binding peptides. We anticipate this screening result will also be extremely useful in the development of inhibitors or drug delivery systems targeting polysaccharides as well as further investigations into the function of carbohydrates in vivo. (c) 2008 Elsevier Ltd. All rights reserved.