Raman spectra of amino acids and their aqueous solutions

Zhu, Guangyong; Zhu, Xun; Fan, Qi; Wan, Xueliang

doi:10.1016/j.saa.2010.12.079

Cited by 422 publications

(423 citation statements)

References 26 publications

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“…These changes show the interaction of these two amino acids with Ade molecule is quite well. The observed blue shift in neat amino acids, assigned as combination of COO À symmetric stretch and in-plane twist of carbon using Gauss View software [23] as well as in literature [32], might be due to significant amount of charge transfer from the amino Fig. 4.…”

Section: Methodsmentioning

confidence: 99%

Monitoring potential molecular interactions of adenine with other amino acids using Raman spectroscopy and DFT modeling

Singh

Donfack

Srivastava

et al. 2015

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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Section: Methodsmentioning

confidence: 99%

Monitoring potential molecular interactions of adenine with other amino acids using Raman spectroscopy and DFT modeling

Singh

Donfack

Srivastava

et al. 2015

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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“…However, implementation of these spectroscopic methods is not an easy task. Recently, Zhu G. et al [1] give an overview of measured Raman spectra of solid amino acids and their aqueous solutions, but today, a database, which would include the vibrational spectra of all amino acids, measured under the same, well-defined and reproducible experimental conditions is not exist.…”

Section: Introductionmentioning

confidence: 99%

Raman study of L-Asparagine and L-Glutamine molecules adsorbed on aluminum films in a wide frequency range

Golichenko¹

2017

Semicond. Phys. Quantum Electron. Optoelectron.

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Abstract. Using micro-Raman spectroscopy, a detailed study of vibrational spectra of L-Asparagine and L-Glutamine amino acids adsorbed on aluminum foils were carried out within the frequency range 80…3500 cm -1 under different excitation wavelengths. On the basis of detailed analysis of Raman spectra of the mentioned above amino acids and data of DFT-calculations of normal modes and isotopic substitution for these analytes available in literature, interpretation of amino acids vibrational bands were performed. The polarized Raman spectra of studied amino acids indicate different ordering of polycrystalline structure in distinct spots on the sample. The most significant variations of ratios between polarized bands are principally observed for deformation vibrations of NH 2 , COO -and CH 2 groups within entire "fingerprint" range and valence vibrations of CC and CN bonds within the range 1000…1100 cm -1 .

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“…Unfortunately, this method often fails inside molecularly rich environments such as tissues consisting of varied components due to overlap of Raman bands that mask the useful information and hinder the ability for accurate and precise characterization. [8][9][10] As noted in a recent review paper, vibrational spectroscopic methods have been widely explored for analysis of various pathologies and organ systems, but as yet, "none have entered routine clinical practice." 2 A 2015 review article concludes that if the combination of vibrational spectroscopy and chemometric analysis is to be successfully transferred into clinical practice more extensive studies are needed.…”

Section: Introductionmentioning

confidence: 99%

Differential laser-induced perturbation Raman spectroscopy: a comparison with Raman spectroscopy for analysis and classification of amino acids and dipeptides

2015

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Abstract. Differential-laser induced perturbation spectroscopy (DLIPS) is a new spectral analysis technique for classification and identification, with key potential applications for analysis of complex biomolecular systems. DLIPS takes advantage of the complex ultraviolet (UV) laser-material interactions based on difference spectroscopy by coupling low intensity UV laser perturbation with a traditional spectroscopy probe. Here, we quantify the DLIPS performance using a Raman scattering probe in classification of basic constituents of collagenous tissues, namely, the amino acids glycine, L-proline, and L-alanine, and the dipeptides glycine-glycine, glycinealanine and glycine-proline and compare the performance to a traditional Raman spectroscopy probe via several multivariate analyses. We find that the DLIPS approach yields an ∼40% improvement in discrimination among these tissue building blocks. The effects of the 193-nm perturbation laser are further examined by assessing the photodestruction of targeted material molecular bonds. The DLIPS method with a Raman probe holds promise for future tissue diagnosis, either as a stand-alone technique or as part of an orthogonal biosensing scheme. © The Authors. Published by SPIE under a Creative Commons Attribution 3.0 Unported License. Distribution or reproduction of this work in whole or in part requires full attribution of the original publication, including its DOI.

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Raman spectra of amino acids and their aqueous solutions

Cited by 422 publications

References 26 publications

Monitoring potential molecular interactions of adenine with other amino acids using Raman spectroscopy and DFT modeling

Monitoring potential molecular interactions of adenine with other amino acids using Raman spectroscopy and DFT modeling

Raman study of L-Asparagine and L-Glutamine molecules adsorbed on aluminum films in a wide frequency range

Differential laser-induced perturbation Raman spectroscopy: a comparison with Raman spectroscopy for analysis and classification of amino acids and dipeptides

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