(S)-2-(4-(2-(tert-butoxycarbonylamino)-3-methoxy-3-oxopropyl)phenylamino)benzoic acid | 643018-84-2

• 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: (S)-2-(4-(2-(tert-butoxycarbonylamino)-3-methoxy-3-oxopropyl)phenylamino)benzoic acid
• 英文别名: N-[(tert-butoxy)carbonyl]-4-[(2-carboxyphenyl)amino]-L-phenylalanine methyl ester；2-[4-[(2S)-3-methoxy-2-[(2-methylpropan-2-yl)oxycarbonylamino]-3-oxopropyl]anilino]benzoic acid
• CAS: 643018-84-2
• 化学式: C₂₂H₂₆N₂O₆
• 分子量: 414.458
• InChiKey: SFCHQZSGUHNWPW-SFHVURJKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.74
• 重原子数：
  30.0
• 可旋转键数：
  7.0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  113.96
• 氢给体数：
  3.0
• 氢受体数：
  6.0

反应信息

• 作为反应物：
  描述：

  (S)-2-(4-(2-(tert-butoxycarbonylamino)-3-methoxy-3-oxopropyl)phenylamino)benzoic acid 在 sodium hydroxide 、 PPA 作用下， 以 叔丁醇 为溶剂， 反应 25.0h， 生成 (2S)-2-{[(tert-butoxy)carbonyl]amino}-3-(9,10-dihydro-9-oxoacridin-2-yl)propanoic acid
  参考文献：
  名称：

  的合成ñ - [（叔丁氧基）羰基] -3-（9,10-二氢-9- oxoacridin -2-基）-L-丙氨酸，新型荧光氨基酸衍生物

  摘要：

  描述了一种新的，高度荧光的氨基酸及其在肽研究中有用的受保护衍生物的简单合成。所获得的衍生物N -[（叔丁氧基）羰基] -3-（9,10-二氢-9-氧杂cri啶-2-基）-L-丙氨酸（6）显示出强烈的长波吸收（360 nm以上） ）和发射（400 nm以上）。被研究化合物的荧光量子产率非常高，因此可以用作灵敏的分析探针，例如，用于分析肽构象。

  DOI：

  10.1002/hlca.200390275
• 作为产物：
  描述：

  Boc-4-氨基-L-苯丙氨酸 在 氯化亚砜 、 铜 、 potassium carbonate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 5.0h， 生成 (S)-2-(4-(2-(tert-butoxycarbonylamino)-3-methoxy-3-oxopropyl)phenylamino)benzoic acid
  参考文献：
  名称：

  Tryptophan-based fluorophores for studying protein conformational changes

  摘要：

  With the continuing interest in deciphering the interplay between protein function and conformational changes, small fluorescence probes will be especially useful for tracking changes in the crowded protein interior space. Presently, we describe the potential utility of six unnatural amino acid fluorescence donors structurally related to tryptophan and show how they can be efficiently incorporated into a protein as fluorescence probes. We also examine the various photophysical properties of the new Trp analogues, which are significantly redshifted in their fluorescence spectra relative to tryptophan. In general, the Trp analogues were well tolerated when inserted into Escherichia coli DHFR, and did not perturb enzyme activity, although substitution for Trp22 did result in a diminution in DHFR activity. Further, it was demonstrated that D and E at position 37 formed efficient FRET pairs with acridon-2-ylalanine (Acd) at position 17. The same was also true for a DHFR construct containing E at position 79 and Acd at position 17. Together, these findings demonstrate that these tryptophan analogues can be introduced into DHFR with minimal disruption of function, and that they can be employed for the selective study of targeted conformational changes in proteins, even in the presence of unmodified tryptophans. (C) 2014 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2014.09.015

文献信息

• Minimalist Probes for Studying Protein Dynamics: Thioamide Quenching of Selectively Excitable Fluorescent Amino Acids
  作者：Jacob M. Goldberg、Lee C. Speight、Mark W. Fegley、E. James Petersson

  DOI：10.1021/ja3005094

  日期：2012.4.11

  Fluorescent probe pairs that can be selectively excited in the presence of Trp and Tyr are of great utility in studying conformational changes in proteins. However, the size of these probe pairs can restrict their incorporation to small portions of a protein sequence where their effects on secondary and tertiary structure can be tolerated. Our findings show that a thioamide bond-a single atom substitution of the peptide backbone-can quench fluorophores that are red-shifted from intrinsic protein fluorescence, such as acridone. Using steady-state and fluorescence lifetime measurements, we further demonstrate that this quenching occurs through a dynamic electron-transfer mechanism. In a proof-of-principle experiment, we apply this technique to monitor unfolding in a model peptide system, the villin headpiece HP35 fragment. Thioamide analogues of the natural amino acids can be placed in a variety of locations in a protein sequence, allowing one to make a large number of measurements to model protein folding.