N-((9-fluorenylmethoxy)carbonyl)-[1-13C]-L-isoleucine | 960525-49-9

• 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: N-((9-fluorenylmethoxy)carbonyl)-[1-13C]-L-isoleucine
• 英文别名: Fmoc-1-13C-Ile-OH
• CAS: 960525-49-9
• 化学式: C₂₁H₂₃NO₄
• 分子量: 354.407
• InChiKey: QXVFEIPAZSXRGM-NBAJOAQZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.02
• 重原子数：
  26.0
• 可旋转键数：
  6.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  75.63
• 氢给体数：
  2.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  N-((9-fluorenylmethoxy)carbonyl)-[1-13C]-L-isoleucine 在 盐酸 、 重氧水 作用下， 以 1,4-二氧六环 、 水 为溶剂， 反应 64.0h， 生成 N-((9-fluorenylmethoxy)carbonyl)-[1-13C]-L-isoleucine
  参考文献：
  名称：

  A Simple and Economical Method for the Production of ¹³C,¹⁸O-Labeled Fmoc-Amino Acids with High Levels of Enrichment:  Applications to Isotope-Edited IR Studies of Proteins

  摘要：

  Isotope-edited IR of proteins has generated considerable interest. Double labeling with C-13 and O-18 with high levels of isotopic enrichment is required for residue-specific resolution. Current methods for the preparation of doubly labeled amino acids give modest O-18 enrichment, limiting the utility of the approach. We report a simple and economical method for preparing C-13,O-18-doubly labeled N-(9-fluorenylmethoxycarbonyl)-amino acids with high levels of enrichment for residues that do not require acid-labile side-chain protecting groups.

  DOI：

  10.1021/ol701913p
• 作为产物：
  描述：

  、 氯甲酸-9-芴基甲酯 在 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 1.5h， 以0.413 g的产率得到N-((9-fluorenylmethoxy)carbonyl)-[1-13C]-L-isoleucine
  参考文献：
  名称：

  IR Study of Cross-Strand Coupling in a β-Hairpin Peptide Using Isotopic Labels

  摘要：

  Model beta-hairpin peptides can be used to develop understanding of fundamental elements of beta-sheet secondary structure formation and stability. We have studied two 13C-labeled variants of a beta-hairpin peptide modified from a design originally proposed by Gellman: Arg-Tyr-Val-Glu-Val-Aib-Gly-Lys-Lys-Ile-Leu-Gln. (In this peptide, the two italicized residues form a beta-turn, while 13C-labels are on the amide C=O of Val3, Lys8 in HBG-L and Val3, Ile10 in HBG-S.) Both these peptides are labeled on opposite strands of the hairpin, but differ in the labeling pattern. One (HBG-L) forms a large (14-atom) H-bonded ring of labeled C=Os, while the other (HBG-S) forms a small (10-atom) H-bonded ring. These impact the amide I infrared spectra, with HBG-L having a 13C frequency and intensity higher than that of HBG-S, in good agreement with our spectral simulations based on quantum mechanically derived force fields. The thermal behavior of both peptides yields a broad thermal transition and lacks an isosbestic point. The 13C band for HBG-L has the largest intensity change with temperature, distinct from the 12C change and the HBG-S 13C change.

  DOI：

  10.1021/ja043007f

文献信息

• Cross-Strand Coupling of a β-Hairpin Peptide Stabilized with an Aib-Gly Turn Studied Using Isotope-Edited IR Spectroscopy
  作者：Rong Huang、Vladimir Setnička、Marcus A. Etienne、Joohyun Kim、Jan Kubelka、Robert P. Hammer、Timothy A. Keiderling

  DOI：10.1021/ja0736414

  日期：2007.11.1

  Isotope-edited IR spectroscopy was used to study a series of singly and doubly C-13=O-labeled beta-hairpin peptides stabilized by an Aib-Gly turn sequence. The double-labeled peptides have amide I' IR spectra that show different degrees of vibrational coupling between the C-13-labeled amides due to variations in the local geometry of the peptide structure. The single-labeled peptides provide controls to determine frequencies characteristic of the diagonal force field (FF) contributions at each position for the uncoupled C-13=O modes. Separation of diagonal FF and coupling effects on the spectra are used to explain the cross-strand labeled spectral patterns. DFT calculations based on an idealized model beta-hairpin peptide correctly predict the vibrational coupling patterns. Extending these model results by consideration of frayed ends and the hairpin conformational flexibility yields an alternate interpretation of details of the spectra. Temperature-dependent isotopically labeled IR spectra reveal differences in the thermal stabilities of the individual isotopically labeled sites. This is the first example of using an IR-based isotopic labeling technique to differentiate structural transitions at specific sites along the peptide backbone in model beta-hairpin peptides.