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

Cheng, Dan; Cai, Wensheng; Shao, Xueguang

doi:10.1177/0003702818769410

Cited by 24 publications

(15 citation statements)

References 57 publications

(85 reference statements)

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“…8 that, with increasing temperature, the intensity for the spectra of S 0 and S 1 increased but that for S 2 decreased, indicating clearly that more OH of S 0 and S 1 was formed but that of S 2 was dissociated. The result was consistent with the previous studies, that was the larger water clusters dissociated into smaller ones with the increasing temperature 25,26,31 . The temperature effect on S 0 , S 1 and S 2 could be obtained by comparing the slope in the Fig.…”

Section: Resultssupporting

confidence: 93%

Understanding hyaluronic acid induced variation of water structure by near-infrared spectroscopy

Dong

Guo²,

et al. 2020

Sci Rep

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In order to understand the hydration effect of hyaluronic acid (HA) in aqueous solution, near-infrared (NIR) spectroscopy was used to investigate the HA aqueous solutions at different concentrations and temperature. As HA concentration was raised, there was a nonlinear change in absorption value in the first overtone region of OH, indicating the changes of hydration water. A reconstructed spectrum based on principal component analysis (PCA) was established and analyzed with the concept of aquaphotomics. The results showed that HA acted as a structure maker to make water molecules arranged in order. Water species with two hydrogen bonds (S 2 ) and three hydrogen bonds (S 3 ) showed the decrease at low concentration range of 0-40 mg/mL, but increased at higher concentration, indicating the difference in water species at different HA concentration. Meanwhile, HA had the ability to improve the thermal stability of water structure, suggesting a potential bio-protective function. this study provides a unique perspective on the molecular interactions between HA and water molecules, which is helpful for understanding the role of HA in life process and may serve as the basis for HA applications.Hyaluronic acid (HA) is a natural polysaccharide and one of the main component of the extracellular matrix 1 . It is widely distributed in various tissues and organs of animals as well as the capsules of some bacteria, and plays a significant role in life process 1 . Due to its high water retaining capacity, biocompatibility and non-immunogenicity, HA is an attractive material for various cosmetic, food and medical applications 2-4 .It is known that the structure and morphology of polysaccharides are strongly influenced by water molecules via controlling their conformations, various forms of aggregation, thermal properties and kinetics 5,6 . In this respect, the knowledge of the interaction between water and polysaccharide and the hydrated structure is of high importance for understanding its performance in the application. Studies on HA hydration have been reported by using various experimental techniques, including nuclear magnetic resonance (NMR) 7 , viscometry 8 , ultrasonic and densitometry analyses 9 , thermal analysis 10,11 , spectroscopic techniques 12-14 , and by means of computer simulations 15 . A complex relationship between HA and water molecules was partly discovered that the macroscopic properties of HA are significantly dependent on its degree of hydration and the function of HA relies on the hydration capacity 4,16-18 .Analysis of the hydration water in aqueous solution is challenging, and the structural changes in water induced by HA are yet to be fully understood. Near-infrared (NIR) spectroscopy, as a powerful analytical method, has unique advantages in studies of molecular structure and interaction [19][20][21][22] . It mainly reflects the overtones and combination modes of functional groups containing hydrogen atoms, such as CH, OH and NH, which play a significant role in chemical bonding and other chemical ph...

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Section: Resultssupporting

confidence: 93%

Understanding hyaluronic acid induced variation of water structure by near-infrared spectroscopy

Dong

Guo²,

et al. 2020

Sci Rep

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“…Due to the sensitivity of NIR spectra to water structures, the spectral changes of water under different perturbations can be a probe to reveal the interactions in aqueous solutions. The interaction of water and bio-organisms including carbohydrate molecules and oligopeptide was investigated using the NIR spectra of aqueous solutions measured at different concentrations and temperatures [30,31,[38][39][40][41]. The spectral components related to different water structures were obtained from the NIR spectra.…”

Section: Interaction Of Water and Solutesmentioning

confidence: 99%

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

2022

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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.

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“…Temperaturedependent NIR spectroscopy and independent component analysis (ICA) were employed to study the interaction between oligopeptide, K 5 (penta-lysine) and D 5 (penta-aspartic acid), and water in aqueous solution. 5 The spectra of the solutions with different concentration were measured at temperature from 30 to 90 C with a step of 5 C. By enhancing the resolution of the spectra with continuous wavelet transform (CWT), the spectral information of NH, CH 2 , and OH groups was observed. Figure 1 shows the original and transformed NIR spectra of D 5 , K 5 solution, and H 2 O at 30, 60, and 90 C, respectively.…”

Section: Development and Resultsmentioning

confidence: 99%

Temperature-dependent near-infrared spectroscopy for studying the interactions in protein aqueous solutions

et al. 2019

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Temperature-dependent near-infrared spectroscopy has been developed for studying quantitative and structural analysis, as well as the molecular interactions. Taking the advantage of the temperature effect on hydrogen bonding, the technique has shown its potential in analyzing the interactions in aqueous solutions. In our recent studies, the structural changes in homo-oligopeptides K5 (penta-lysine), D5 (penta-aspartic acid), and protein (ovalbumin) aqueous solutions were studied by temperature-dependent near-infrared spectroscopy. The thermodynamics and their interaction with water were analyzed with the help of the chemometric methods including continuous wavelet transform, independent component analysis, two-dimensional (2D) correlation analysis, and Gaussian fitting. The results show that the oligopeptide in aqueous solution improves the thermal stability of the water species, and K5 has stronger interaction with water than D5. In the gelation of ovalbumin, the change of the water species with two hydrogen bonds (S2) follows the same phases as the protein. S2 maintains the stability of the protein in native and molten globule states, and the weakening of the hydrogen bond in S2 by high temperature results in the destruction of the hydration shell and makes the ovalbumin clusters form a gel structure.

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

Cited by 24 publications

References 57 publications

Understanding hyaluronic acid induced variation of water structure by near-infrared spectroscopy

Understanding hyaluronic acid induced variation of water structure by near-infrared spectroscopy

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

Temperature-dependent near-infrared spectroscopy for studying the interactions in protein aqueous solutions

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