Understanding the Molecular Interaction in Solutions by Chemometric Resolution of Near−Infrared Spectra

Shao, Xueguang; Cui, Xiaoyu; Liu, Yan; Xia, Zhenzhen; Cai, Wensheng

doi:10.1002/slct.201700939

Cited by 24 publications

(11 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In IC2, IC3, and IC4, one main peak is obtained for each IC, which is located at 7072, 6968, and 6826 cm À1 , respectively. According to the previous works, [19][20][21]26,31,[33][34][35][36][37]53 the peaks correspond to the absorption of n 1 þ n 3 of the differently hydrogen-bonded OH, i.e., the free OH (S 0 ), OH with one hydrogen bond (S 1 ) and OH with two hydrogen bonds (S 2 ), respectively. The positive peaks around 7200 cm À1 in IC4 may also be the information of water vapor.…”

Section: Structural Changes Of Water Induced By D 5 and Kmentioning

confidence: 87%

“…33 Furthermore, the methods for resolving the spectral components of different water species and the pure component spectra from the measured spectra of aqueous solution were developed to study the molecular interaction in solutions and the effect of the solute on water structure. 34,35 In these studies, the feasibility for analyzing the molecular interactions using temperature-dependent NIR spectra was proved and water can be a probe for the analysis. Similar works were also reported such as the early diagnosis of amyloidosis 36 and estrus detection of female giant panda 37 using NIR spectroscopy.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Understanding the Interaction Between Oligopeptide and Water in Aqueous Solution Using Temperature-Dependent Near-Infrared Spectroscopy

2018

Self Cite

View full text Add to dashboard Cite

Investigating the interaction between oligopeptide and water is essential for understanding the structure, dynamics and function of proteins. Temperature-dependent near-infrared (NIR) spectroscopy and independent component analysis (ICA) were employed to study the interaction between oligopeptide and water in aqueous solution. The NIR spectra of two homo-oligopeptides, penta-aspartic acid (D) and penta-lysine (K), in aqueous solution of different concentration were measured at different temperature (30-90 ℃). Independent component analysis was performed to extract the spectral information that changes with temperature. The independent components (ICs) representing the spectral information of NH and CH groups were obtained. Compared with D, the two groups in K change significantly at higher temperature. The result may suggest that K has stronger interaction with water than D. Moreover, three ICs that contain the spectral information of the water species with no (S), one (S), and two (S) hydrogen-bonds were obtained. It was shown that the spectral intensity of S and S increases while that of S decreases with the temperature, and the changes of oligopeptide solutions are weaker than those of pure water. The results indicate that water structure is sensitive to temperature and the oligopeptide in aqueous solution improves the thermal stability of the water species. When oligopeptide is added, the spectral intensity of S and S decreases and that of S increases for D solution, but the intensity of all the three species decreases for K solution. Furthermore, the concentration effect of K was found to be stronger than D. The result may reveal that D combines with water molecule through forming one hydrogen bond but K interacts with water through a different way.

show abstract

Section: Structural Changes Of Water Induced By D 5 and Kmentioning

confidence: 87%

Section: Introductionmentioning

confidence: 99%

Understanding the Interaction Between Oligopeptide and Water in Aqueous Solution Using Temperature-Dependent Near-Infrared Spectroscopy

2018

Self Cite

View full text Add to dashboard Cite

show abstract

“…Through the variation of the spectra with the concentration, it was revealed that ethanol promotes the formation of water clusters. To obtain more spectral information of the interactions of water and ethanol, a new method was proposed based on the rotation of the loadings in principal component analysis (PCA) [42]. The calculated spectra were found to be more reliable to reflect the structures in the mixture, from which the spectral features of different water species (S 0 -S 4 ), ethanol clusters, and the interaction of OH and CH groups were observed.…”

Section: Interaction Of Water and Solutesmentioning

confidence: 99%

Chemometrics: An Excavator in Temperature-Dependent Near-Infrared Spectroscopy

2022

Self Cite

View full text Add to dashboard Cite

Temperature-dependent near-infrared (NIR) spectroscopy has been developed and taken as a powerful technique for analyzing the structure of water and the interactions in aqueous systems. Due to the overlapping of the peaks in NIR spectra, it is difficult to obtain the spectral features showing the structures and interactions. Chemometrics, therefore, is adopted to improve the spectral resolution and extract spectral information from the temperature-dependent NIR spectra for structural and quantitative analysis. In this review, works on chemometric studies for analyzing temperature-dependent NIR spectra were summarized. The temperature-induced spectral features of water structures can be extracted from the spectra with the help of chemometrics. Using the spectral variation of water with the temperature, the structural changes of small molecules, proteins, thermo-responsive polymers, and their interactions with water in aqueous solutions can be demonstrated. Furthermore, quantitative models between the spectra and the temperature or concentration can be established using the spectral variations of water and applied to determine the compositions in aqueous mixtures.

show abstract

“…The influence of temperature on the structure of Ara h1 was characterized by an aquagram. The characteristic absorption bands of the Ara h1 aqueous solution during temperature change were shown in Table 2 (32)(33)(34)(35)(36)(37)(38)(39). The aquagram with the 12 WAMACS was shown in Figure 8.…”

Section: Ara H1 Aquagram Analysismentioning

confidence: 99%

Research on the Structure of Peanut Allergen Protein Ara h1 Based on Aquaphotomics

et al. 2021

View full text Add to dashboard Cite

Peanut allergy is becoming a life-threatening disease that could induce severe allergic reactions in modern society, especially for children. The most promising method applied for deallergization is heating pretreatment. However, the mechanism from the view of spectroscopy has not been illustrated. In this study, near-infrared spectroscopy (NIRS) combined with aquaphotomics was introduced to help us understand the detailed structural changes information during the heating process. First, near-infrared (NIR) spectra of Ara h1 were acquired from 25 to 80°C. Then, aquaphotomics processing tools including principal component analysis (PCA), continuous wavelet transform (CWT), and two-dimensional correlation spectroscopy (2D-COS) were utilized for better understanding the thermodynamic changes, secondary structure, and the hydrogen bond network of Ara h1. The results indicated that about 55°C could be a key temperature, which was the structural change point. During the heating process, the hydrogen bond network was destroyed, free water was increased, and the content of protein secondary structure was changed. Moreover, it could reveal the interaction between the water structure and Ara h1 from the perspective of water molecules, and explain the effect of temperature on the Ara h1 structure and hydrogen-bonding system. Thus, this study described a new way to explore the thermodynamic properties of Ara h1 from the perspective of spectroscopy and laid a theoretical foundation for the application of temperature-desensitized protein products.

show abstract

Understanding the Molecular Interaction in Solutions by Chemometric Resolution of Near−Infrared Spectra

Cited by 24 publications

References 33 publications

Understanding the Interaction Between Oligopeptide and Water in Aqueous Solution Using Temperature-Dependent Near-Infrared Spectroscopy

Understanding the Interaction Between Oligopeptide and Water in Aqueous Solution Using Temperature-Dependent Near-Infrared Spectroscopy

Chemometrics: An Excavator in Temperature-Dependent Near-Infrared Spectroscopy

Research on the Structure of Peanut Allergen Protein Ara h1 Based on Aquaphotomics

Contact Info

Product

Resources

About