Two-dimensional IR Correlation Spectroscopy Research Articles

Verification of Ganoderma (lingzhi) commercial products by Fourier Transform infrared spectroscopy and two-dimensional IR correlation spectroscopy

Ganoderma commercial products are typically based on two sources, raw material (powder form and/or spores) and extract (water and/or solvent). This study compared three types of Ganoderma commercial products using 1 Dimensional Fourier Transform infrared and second derivative spectroscopy. The analyzed spectra of Ganoderma raw material products were compared with spectra of cultivated Ganoderma raw material powder from different mushroom farms in Malaysia. The Ganoderma extract product was also compared with three types of cultivated Ganoderma extracts. Other medicinal Ganoderma contents in commercial extract product that included glucan and triterpenoid were analyzed by using FTIR and 2DIR. The results showed that water extract of cultivated Ganoderma possessed comparable spectra with that of Ganoderma product water extract. By comparing the content of Ganoderma commercial products using FTIR and 2DIR, product content profiles could be detected. In addition, the geographical origin of the Ganoderma products could be verified by comparing their spectra with Ganoderma products from known areas. This study demonstrated the possibility of developing verification tool to validate the purity of commercial medicinal herbal and mushroom products.

The Hydrogen-Bonded 2-Pyridone Dimer Model System. 1. Combined NMR and FT-IR Spectroscopy Study

2-Pyridone (PD), converting to 2-hydroxypyridine (HP) through a lactam-lactim isomerization mechanism, can form three different cyclic dimers by hydrogen bond formation: (PD)(2), (PD-HP), and (HP)(2). We investigate the complexation chemistry of pyridone in dichloromethane-d(2) using a combined NMR and Fourier transform infrared (FT-IR) approach. Temperature-dependent (1)H NMR spectra indicate that at low temperatures (<200 K) pyridone in solution predominantly exists as a cyclic (PD)(2) dimer, in exchange with PD monomers. At higher temperatures a proton exchange mechanism sets in, leading to a collapse of the doublet of (15)N labeled 2-pyridone. Linear FT-IR spectra indicate the existence of several pyridone species, where, however, a straightforward interpretation is hampered by extensive spectral overlap of many vibrational transitions in both the fingerprint and the NH/OH stretching regions. Two-dimensional IR correlation spectroscopy applied on concentration-dependent and temperature-dependent data sets reveals the existence of the (PD)(2) cyclic dimer, of PD-CD(2)Cl(2) solute-solvent complexes, and of PD-PD chainlike dimers. Regarding the difference in effective time scales of the NMR and FT-IR experiments, milliseconds vs (sub)picoseconds, the cyclic dimers (PD-HP) and (HP)(2), and the chainlike conformations HP-PD, may function as intermediates in reaction pathways through which the protons exchange between PD units in cyclic (PD)(2).

Spectroscopic and Computational Insight into the Intermolecular Interactions between Zwitter‐Type Ionic Liquids and Water Molecules

Geometric and conformational changes of zwitter-type ionic liquids (ZILs) due to hydrogen-bonding interactions with water molecules are investigated by density functional theory (DFT), two-dimensional IR correlation spectroscopy (2D IR COS), and pulsed-gradient spin-echo NMR (PGSE NMR). Simulation results indicate that molecular structures in the optimized states are strongly influenced by hydrogen bonding of water molecules with the sulfonate group or imidazolium and pyrrolidinium rings of 3-(1-methyl-3-imidazolio)propanesulfonate (1) and 3-(1-methyl-1-pyrrolidinio)propanesulfonate (2), respectively. Concentration-dependent 2D IR COS reveals kinetic conformational changes of the two ZIL-H(2)O systems attributable to intermolecular interactions, as well as the interactions of sulfonate groups and imidazolium or pyrrolidinium rings with water molecules. The dramatic changes in the (1)H self-diffusion coefficients elucidate the formation of proton-conduction pathways consisting of ZIL networks. In ZIL domains, protons are transferred by a Grotthuss-type mechanism through formation, breaking, and restructuring of bonds between ZILs and H(2)O, leading to an energetically favorable state. The simulation and experimental investigations delineated herein provide a perspective to understanding the interactions with water from an academic point of view as well as to designing ILs with desired properties from the viewpoint of applications.

Dissimilar Dynamics of Coupled Water Vibrations

Dissimilar dynamics of coupled stretch vibrations of a water molecule are revealed by two-dimensional IR correlation spectroscopy. These are caused by essentially non-Gaussian fluctuations of the electric field exerted by the environment on the individual OH stretch vibrations. Non-Gaussian statistics of the individual site frequency fluctuations results in distinctively different dephasing of the symmetric and asymmetric eigenmodes. This phenomenon can only be described if the assumption of Gaussian dynamics in the traditional theories is abandoned.

On the protonation of oxo- and hydroxo-groups of the goethite (α-FeOOH) surface: A FTIR spectroscopic investigation of surface O–H stretching vibrations

The O–H stretching region of goethite particles evaporated at different levels of acidity was investigated by Attenuated Total Reflectance (ATR)-Fourier Transform InfraRed (FTIR) spectroscopy. Two-dimensional IR Correlation Spectroscopy was used to identify correlations between different sets of discrete surface OH stretches and a Multivariate Curve Resolution analysis was used to resolve the predominant spectral components. Two dominant groups of hydroxyls were identified on the basis of their differences in proton affinity. Group I hydroxyls appear as two 3698/3541 and 3660/3490 cm −1 band pairs. Group II hydroxyls are manifested through the 3648 and 3578 cm −1 bands at greater levels of surface proton loading. There is consequently no correlation between O–H stretching frequencies and proton affinity. Groups I and II were assigned to mostly singly- (–OH) and doubly- (μ-OH) coordinated hydroxyls, respectively. Stretches arising from triply-coordinated (μ 3-OH) are proposed to be embedded within the dominant O–H band of bulk goethite. The possibility that these sites contribute to Group I and II hydroxyls should, however, not be entirely dismissed without further investigations. A reexamination of Temperature Programmed Desorption (TPD)-FTIR data of one goethite sample evaporated from alkaline conditions [Boily J.-F., Szanyi J., Felmy A. R. (2006) A combined FTIR and TPD study on the bulk and surface dehydroxylation and decarbonation of synthetic goethite. Geochim. Cosmochim. Acta 70, 3613–3624] provided further constraints to this band assignment by providing clues to the network of surface hydrogen bonds. Important cooperative effects between hydrogen-bonded surface hydroxyls are suggested to play a crucial role on the variations of the position and intensity of discrete O–H stretching bands as a function of protonation level and temperature.

Simulation of FT-IR spectra and 2D-COS analysis for the H/D exchange of two related ligands

Two-dimensional IR correlation spectroscopy (2D-COS) is a relatively novel method that provides the analysis of infrared spectra with the capacity to differentiate overlapping peaks and to distinguish between in-phase and out-of-phase spectral responses. The technique is becoming popular for protein dynamic studies, like H/D exchange attenuated total reflectance Fourier transform-infrared (ATR-FT-IR) spectroscopy. The use of this technique provides the capability to resolve the dynamic molecular events that occur upon H → D exchange of accessible amide protons and exchangeable protons within side chain (Arg, Tyr) that are commonly overlapped. The value of the use of simulated spectra to generate the 2D-COS plots is that it allows for confirmation of the existence of the auto-peaks and its correlations. Because of this, we have employed the use of simulated spectra originated from backbone vibrational contributions such as amide I, I′, II and II′ bands for a case study presented herein. Intensity, bandwidth, and band position were the parameters used to study their variation in the correlation plots during a typical H/D exchange ATR-FT-IR experiment. These simulations are compared with experimental spectral data from ATR-FT-IR analysis in order to separate the backbone contribution from the highly overlapped side chain contributions (mainly Arg and Tyr).

Response to “On the Application of Two-Dimensional IR Correlation Spectroscopy: Some Critical Comments”

Response to “On the Application of Two-Dimensional IR Correlation Spectroscopy: Some Critical Comments”

On the Application of Two-Dimensional IR Correlation Spectroscopy: Some Critical Comments

On the Application of Two-Dimensional IR Correlation Spectroscopy: Some Critical Comments

Two-dimensional IR correlation spectroscopy: sequential events in the unfolding process of the lambda cro-V55C repressor protein.

A question often posed in protein folding/unfolding studies is whether the process is fully cooperative or whether it contains sequential elements. To address this question, one needs tools capable of resolving different events. It seems that, at least in certain cases, two-dimensional (2D) IR correlation spectroscopy can provide answers to this question. To illustrate this point, we have turned to the Cro-V55C dimer of the lambda Cro repressor, a protein known to undergo thermal unfolding in two discrete steps through a stable equilibrium intermediate. The secondary structure of this intermediate is compatible with that of a partially unfolded protein and involves a reorganization of the N terminus, whereas the antiparallel beta-ribbon formed by the C-terminal part of each subunit remains largely intact. To establish whether the unfolding process involves sequential events, we have performed a 2D correlation analysis of IR spectra recorded over the temperature range of 20-95 degrees C. The 2D IR correlation analysis indeed provides evidence for a sequential formation of the stable intermediate, which is created in three (closely related) steps. A first step entails the unfolding of the short N-terminal beta-strand, followed by the unfolding of the alpha-helices in a second step, and the third step comprises the reorganization of the remaining beta-sheet and of some unordered segments in the protein. The complete unfolding of the stable intermediate at higher temperatures also undergoes sequential events that ultimately end with the breaking of the H bonds between the two beta-strands at the dimer interface.