Raman Spectroscopy and Its Modifications Applied to Biological and Medical Research

Allakhverdiev, Elvin S.; Khabatova, Venera V.; Kossalbayev, Bekzhan D.; Zadneprovskaya, Elena V.; Rodnenkov, O. V.; Martynyuk, T V; Максимов, Г. В.; Alwasel, Saleh; Tomo, Tatsuya; Allakhverdiev, Suleyman I.

doi:10.3390/cells11030386

Cited by 48 publications

(28 citation statements)

References 135 publications

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“…No significant changes were observed in the BSA spectra, and the only change was observed in the region of 1570 cm−1. This change is associated with the degradation of α-helices [ 46 ]. Changes in the structure of α-helices usually lead to the partial denaturation or aggregation of molecules.…”

Section: Discussionmentioning

confidence: 99%

Effect of Laser-Induced Optical Breakdown on the Structure of Bsa Molecules in Aqueous Solutions: An Optical Study

et al. 2022

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The influence of laser radiation of a typical surgical laser on the physicochemical properties of the Bovine Serum Albumin (BSA) protein was studied. It was established that the physicochemical characteristics of optical breakdown weakly depend on the concentration of protein molecules. At the same time, the patterns observed for an aqueous solution of BSA irradiated with a laser for different time periods were extremely similar to the classical ones. It was established that after exposure to laser radiation, the optical density of protein solutions increases. At the same time, the intensity of BSA fluorescence due to aromatic amino acid residues decreases insignificantly after exposure to laser radiation. In this case, the position of the excitation and emission maximum does not change, and the shape of the fluorescence spot on 3D maps also does not change significantly. On the Raman spectrum after exposure to laser radiation, a significant decrease in 1570 cm−1 was observed, which indicates the degradation of α-helices and, as a result, partial denaturation of BSA molecules. Partial denaturation did not significantly change the total area of protein molecules, since the refractive index of solutions did not change significantly. However, in BSA solutions, after exposure to laser radiation, the viscosity increased, and the pseudoplasticity of aqueous solutions decreased. In this case, there was no massive damage to the polypeptide chain; on the contrary, when exposed to optical breakdown, intense aggregation was observed, while aggregates with a size of 400 nm or more appeared in the solution. Thus, under the action of optical breakdown induced by laser radiation in a BSA solution, the processes of partial denaturation and aggregation prevail, aromatic amino acid residues are damaged to a lesser extent, and fragmentation of protein molecules is not observed.

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Section: Discussionmentioning

confidence: 99%

Effect of Laser-Induced Optical Breakdown on the Structure of Bsa Molecules in Aqueous Solutions: An Optical Study

et al. 2022

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“…According to data in the literature, in the absence of a nitrogen source in the culture medium, 5–10% of the cells of the filaments of nitrogen-fixing cyanobacteria differentiate into heterocysts within about 24 h [ 50 ]. Heterocysts supply the vegetative cells with fixed nitrogen and receive carbohydrates from them in return [ 51 , 52 ]. This mutual exchange of balanced nutrients is regulated at the gene level to ensure their optimal growth and adaptation for long-term survival.…”

Section: Discussionmentioning

confidence: 99%

Influence of Mo and Fe on Photosynthetic and Nitrogenase Activities of Nitrogen-Fixing Cyanobacteria under Nitrogen Starvation

Sadvakasova

Kossalbayev

Token

et al. 2022

Cells

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The potential of cyanobacteria to perform a variety of distinct roles vital for the biosphere, including nutrient cycling and environmental detoxification, drives interest in studying their biodiversity. Increasing soil erosion and the overuse of chemical fertilizers are global problems in developed countries. The option might be to switch to organic farming, which entails largely the use of biofertilisers. Cyanobacteria are prokaryotic, photosynthetic organisms with considerable potential, within agrobiotechnology, to produce biofertilisers. They contribute significantly to plant drought resistance and nitrogen enrichment in the soil. This study sought, isolated, and investigated nitrogen-fixing cyanobacterial strains in rice fields, and evaluated the effect of Mo and Fe on photosynthetic and nitrogenase activities under nitrogen starvation. Cyanobacterial isolates, isolated from rice paddies in Kazakhstan, were identified as Trichormus variabilis K-31 (MZ079356), Cylindrospermum badium J-8 (MZ079357), Nostoc sp. J-14 (MZ079360), Oscillatoria brevis SH-12 (MZ090011), and Tolypothrix tenuis J-1 (MZ079361). The study of the influence of various concentrations of Mo and Fe on photosynthetic and nitrogenase activities under conditions of nitrogen starvation revealed the optimal concentrations of metals that have a stimulating effect on the studied parameters.

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“…Therefore, Raman spectroscopy is suitable for measurements of heatsensitive biological samples, such as proteins, too. [32,33] This study is aimed to investigate the formation of the His-Ni (II) complex in different conditions using Raman spectroscopy. The use of this technique has not been reported before.…”

Section: Introductionmentioning

confidence: 99%

Identification of histidine‐Ni (II) metal complex by Raman spectroscopy

Pál

Vereš

Holomb

et al. 2022

J Raman Spectroscopy

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Metal ions such as nickel have a strong binding affinity to amino acids and form metal complexes of different geometry. This complex formation is influenced by many factors among others the kind of reactants and their relative concentrations, pH, and its effect on the net charge of the amino acid molecule. In this work, the formation of the histidine‐nickel (II) complex in different conditions was examined by Raman spectroscopy. In addition to the experiments, density functional theory (DFT) calculations on histidine‐nickel complexes were performed in order to elucidate the complex formation mechanism and optimal geometry of the structures as well as to investigate their vibrational properties. The Raman measurements showed double peaks at 1272 and 1297 cm−1, and triple peaks at 1322, 1336, and 1355 cm−1 that belong to the metal complex. The geometry optimizations and total energy calculations of His‐Ni (II) complex revealed that the octahedral geometry and the triplet spin state of Ni ion is the energetically favorable structure. This metal complex is formed through the nitrogen atom of the imidazole side chain, the nitrogen atom of the terminal amino group, and the oxygen atom of the carboxyl group. Experiments with pH revealed that the alkaline pH favors while the change of the concentration of the metal ions does not affect the the His‐Ni (II) complex formation.

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Raman Spectroscopy and Its Modifications Applied to Biological and Medical Research

Cited by 48 publications

References 135 publications

Effect of Laser-Induced Optical Breakdown on the Structure of Bsa Molecules in Aqueous Solutions: An Optical Study

Effect of Laser-Induced Optical Breakdown on the Structure of Bsa Molecules in Aqueous Solutions: An Optical Study

Influence of Mo and Fe on Photosynthetic and Nitrogenase Activities of Nitrogen-Fixing Cyanobacteria under Nitrogen Starvation

Identification of histidine‐Ni (II) metal complex by Raman spectroscopy

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