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Special Issue "Recent Advances in Chiroptical Spectroscopy"

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Analytical Chemistry".

Deadline for manuscript submissions: 31 August 2018

Special Issue Editor

Guest Editor
Prof. Dr. Reiko Kuroda

Research Institute for Science and Technology, Tokyo University of Science, 2641 Yamazaki,Noda-shi, Chiba 278-8510 Japan
Website | E-Mail
Interests: chiroptical spectroscopy especially in the condensed phase; chiral recognition, discrimination and enhancement in the solid state; chirality determination mechanism of snail Lymnaea stagnalis by a single gene during the embryogenesis

Special Issue Information

Dear Colleagues,

Chirality is expressed throughout nature, whether microscopic or macroscopic, and animate or inanimate. Examples include molecules, crystals and complex living organisms. From the molecular standpoint, life is totally homochiral; that is, all living organisms on Earth use molecules of a unique invariant handedness: only D- (deoxy) ribose in nucleic acids and only L-amino acids in proteins. Thus, chirality is a key issue in understanding the origin of life on Earth, as well as in agricultural, pharmaceutical and food industries as their biological effects often depend on the chirality of compounds.

The present Special Issue, “Recent Advances in Chiroptical Spectroscopy”, aims to provide comprehensive coverage of the most important and up-to-date methods dealing with polarized light, including their basic principles, instrumentation, and theoretical simulation for application to organic molecules, inorganic molecules, and biomolecules.

Prof. Dr. Reiko Kuroda
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • VCD/ECD/CPL/CD/ROA
  • Instrumentation (condensed phases, fast measurements etc.)
  • Theoretical approaches
  • Biomolecules (proteins/peptides/lipids/nucleic acids/sugars etc.)
  • Organic compounds/liquid crystals/supramolecules
  • Inorganic compounds (transition metal complexes, lanthanides etc.)

Published Papers (4 papers)

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Research

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Open AccessArticle Circular Dichroism in Fluorescence Emission Following the C 1s→π* Excitation and Resonant Auger Decay of Carbon Monoxide
Molecules 2018, 23(7), 1534; https://doi.org/10.3390/molecules23071534
Received: 29 May 2018 / Revised: 14 June 2018 / Accepted: 21 June 2018 / Published: 26 June 2018
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Abstract
Dichroism in angle-resolved spectra of circularly polarized fluorescence from freely-rotating CO molecules was studied experimentally and theoretically. For this purpose, carbon monoxide in the gas phase was exposed to circularly polarized soft X-ray synchrotron radiation. The photon energy was tuned across the C
[...] Read more.
Dichroism in angle-resolved spectra of circularly polarized fluorescence from freely-rotating CO molecules was studied experimentally and theoretically. For this purpose, carbon monoxide in the gas phase was exposed to circularly polarized soft X-ray synchrotron radiation. The photon energy was tuned across the C 1s→π* resonant excitation, which decayed via the participator Auger transition into the CO+ A 2Π state. The dichroic parameter β1 of the subsequent CO+ (A 2Π → X 2Σ+) visible fluorescence was measured by photon-induced fluorescence spectroscopy. Present experimental results are explained with the ab initio electronic structure and dynamics calculations performed by the single center method. Our results confirm the possibility to perform partial wave analysis of the emitted photoelectrons in closed-shell molecules. Full article
(This article belongs to the Special Issue Recent Advances in Chiroptical Spectroscopy)
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Open AccessArticle Long-Time Relaxation of Stress-Induced Birefringence of Microcrystalline Alkali Halide Crystals
Molecules 2018, 23(4), 757; https://doi.org/10.3390/molecules23040757
Received: 26 February 2018 / Revised: 18 March 2018 / Accepted: 21 March 2018 / Published: 25 March 2018
PDF Full-text (20067 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Alkali halide single crystals are most commonly used as the diluent matrix in the tablet method or disk technique for spectroscopic measurements. However, stress-induced birefringence (SIB) of alkali halides as well as intrinsic birefringence manifest during the disk formation process. Thus, the true
[...] Read more.
Alkali halide single crystals are most commonly used as the diluent matrix in the tablet method or disk technique for spectroscopic measurements. However, stress-induced birefringence (SIB) of alkali halides as well as intrinsic birefringence manifest during the disk formation process. Thus, the true chiroptical measurement is disturbed by optical anisotropies (OA) containing SIB and intrinsic birefringence, except in the case of optical homogeneity. SIB is generally larger than intrinsic birefringence and has a value of several thousand millidegrees in the ultraviolet-visible wavelength range, although this varies with disk type. Here, to investigate the SIB origin, alkali halide crystals were examined using polarized light, X-ray diffraction, Fourier-transform infrared, and electron backscattering diffraction spectroscopic measurements. It was found that, after stress release, the SIB exhibited nonlinear long-time relaxation, which roughly converged within several hours, with the only time-invariant intrinsic birefringence remaining being due to OA. This behavior was strongly related to an increase in the quasi-amorphous domain and the generation of an air gap between the crystallite boundaries and their pellets. Further, a straightforward correlation was found between amorphization and an increase in the disk water content caused by deliquescence. Thus, the OA of alkali halide single crystals was found to have two different origins yielding intrinsic birefringence and SIB. Full article
(This article belongs to the Special Issue Recent Advances in Chiroptical Spectroscopy)
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Open AccessArticle Chiral and Molecular Recognition through Protonation between Aromatic Amino Acids and Tripeptides Probed by Collision-Activated Dissociation in the Gas Phase
Molecules 2018, 23(1), 162; https://doi.org/10.3390/molecules23010162
Received: 6 December 2017 / Revised: 6 January 2018 / Accepted: 11 January 2018 / Published: 13 January 2018
Cited by 2 | PDF Full-text (1069 KB) | HTML Full-text | XML Full-text
Abstract
Chiral and molecular recognition through protonation was investigated through the collision-activated dissociation (CAD) of protonated noncovalent complexes of aromatic amino acid enantiomers with l-alanine- and l-serine-containing tripeptides using a linear ion trap mass spectrometer. In the case of l-alanine-tripeptide (AAA),
[...] Read more.
Chiral and molecular recognition through protonation was investigated through the collision-activated dissociation (CAD) of protonated noncovalent complexes of aromatic amino acid enantiomers with l-alanine- and l-serine-containing tripeptides using a linear ion trap mass spectrometer. In the case of l-alanine-tripeptide (AAA), NH3 loss was observed in the CAD of heterochiral H+(d-Trp)AAA, while H2O loss was the main dissociation pathways for l-Trp, d-Phe, and l-Phe. The protonation site of heterochiral H+(d-Trp)AAA was the amino group of d-Trp, and the NH3 loss occurred from H+(d-Trp). The H2O loss indicated that the proton was attached to the l-alanine tripeptide in the noncovalent complexes. With the substitution of a central residue of l-alanine tripeptide to l-Ser, ASA recognized l-Phe by protonation to the amino group of l-Phe in homochiral H+(l-Phe)ASA. For the protonated noncovalent complexes of His enantiomers with tripeptides (AAA, SAA, ASA, and AAS), protonated His was observed in the spectra, except for those of heterochiral H+(d-His)SAA and H+(d-His)AAS, indicating that d-His did not accept protons from the SAA and AAS in the noncovalent complexes. The amino-acid sequences of the tripeptides required for the recognition of aromatic amino acids were determined by analyses of the CAD spectra. Full article
(This article belongs to the Special Issue Recent Advances in Chiroptical Spectroscopy)
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Graphical abstract

Review

Jump to: Research

Open AccessReview UV-Denaturation Assay to Assess Protein Photostability and Ligand-Binding Interactions Using the High Photon Flux of Diamond B23 Beamline for SRCD
Molecules 2018, 23(8), 1906; https://doi.org/10.3390/molecules23081906
Received: 8 June 2018 / Revised: 10 July 2018 / Accepted: 10 July 2018 / Published: 31 July 2018
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Abstract
Light irradiation with high photon flux in the vacuum and far-UV region is known to denature the conformation of biopolymers. Measures are in place at Diamond Light Source B23 beamline for Synchrotron Radiation Circular Dichroism (SRCD) to control and make this effect negligible.
[...] Read more.
Light irradiation with high photon flux in the vacuum and far-UV region is known to denature the conformation of biopolymers. Measures are in place at Diamond Light Source B23 beamline for Synchrotron Radiation Circular Dichroism (SRCD) to control and make this effect negligible. However, UV denaturation of proteins can also be exploited as a novel method for assessing biopolymer photostability as well as ligand-binding interactions. Usually, host–ligand binding interactions can be assessed monitoring CD changes of the host biopolymer upon ligand addition. The novel method of identifying ligand binding monitoring the change of relative rate of UV denaturation using SRCD is especially important when there are very little or insignificant secondary structure changes of the host protein upon ligand binding. The temperature study, another method used to determine molecular interactions, can often be inconclusive when the thermal effect associated with the displacement of the bound solvent molecules by the ligand is also small, making the determination of the binding interaction inconclusive. Herein we present a review on the UV-denaturation assay as a novel method to determine the relative photostability of protein formulations as well as the screening of ligand-binding interactions using the high photon flux Diamond B23 beamline for SRCD. Full article
(This article belongs to the Special Issue Recent Advances in Chiroptical Spectroscopy)
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Title: Protein photostability and ligand binding assay methods using high photon flux of Diamond B23 beamline for SRCD
Type: Review
Author: Rohanah Hussain (Harwell Science Innovation Campus, UK)
Abstract: High photon flux in the vacuum and far UV region is known to denature/degrade biopolymers. Measures are in place at Diamond Light Source Synchrotron Radiation Circular Dichroism (SRCD) B23 beamline to control and make this effect negligible.   However, UV denaturation/degradation can also be exploited as a novel method for assessing biopolymer stability as well as ligand binding interactions. Usually host-ligand binding interactions can be assessed monitoring CD changes of the host upon ligand addition. The novel method of identifying ligand binding monitoring the change of relative UV denaturation using SRCD is especially important when there are very little or insignificant secondary structure changes of the host protein upon ligand binding. The temperature study, another method used to determine molecular interactions can often be inconclusive when the thermal effect, associated with the displacement of the bound solvent molecules by the ligand is also small making the determination of the binding interaction inconclusive. Here we present a review on the novel protein stability and ligand binding assay methods using the high photon flux of SRCD B23 beamline and to discriminate the relative stability of different types of protein folding in different formulations and also in the presence of ligands.
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