Probing chirality of crystals using electron paramagnetic resonance (EPR) spectroscopy

被引：0

作者：

Otis, Gil ^{[1
,2
]}

Aias, Denial ^{[1
,2
]}

Grinberg, Ilya ^{[1
,2
]}

Ruthstein, Sharon ^{[1
,2
]}

Mastai, Yitzhak ^{[1
,2
]}

机构：

[1] Bar Ilan Univ, Dept Chem, IL-5290002 Ramat Gan, Israel

[2] Bar Ilan Univ, Inst Nanotechnol & Adv Mat, IL-5290002 Ramat Gan, Israel

来源：

JOURNAL OF MOLECULAR STRUCTURE | 2024年 / 1297卷

基金：

以色列科学基金会;

关键词：

Chirality; Electron paramagnetic resonance (EPR); Chiral crystals; Chirality measurements; CIRCULAR-DICHROISM SPECTROSCOPY; X-RAY CRYSTALLOGRAPHY; SPIN-RESONANCE; ABSOLUTE-STRUCTURE; BINDING-SITES; PRION PROTEIN; CRYSTALLIZATION; RECOGNITION; POLYMORPHS; MOLECULES;

D O I：

10.1016/j.molstruc.2023.136943

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

One of the most challenging tasks in analytical chemistry is the determination of the chirality (identification of an enantiomeric composition) in solids mainly because of the strict requirements of the pharmaceutical industry for enantiomerically pure drugs. Although there are a few methods available to accomplish enantio-differ-entiation in solids, for example: X-ray diffraction (XRD), Thermogravimetric analysis (TGA), CD spectroscopy, and low-frequency (LF) Raman spectroscopy, this is still very challenging. In this work, we have developed a new method to measure the chirality of crystals, based on electron paramagnetic resonance (EPR) spectroscopy of chiral crystals doped with Cu2+ as the EPR active ion. Here, we demonstrate our approach using a model system ofL- and DL-Histidine crystals doped with Cu2+. We show that EPR measurements of the Cu2+-doped Histidine crystals can accurately determine the chirality and enantiomeric composition of the crystals. We present a very preliminary example of this technique, and we hope that in the future it will be possible to refine and develop this method for many other chiral organic crystal systems.

引用

页数：7

共 55 条

[1] Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy [J].