Drop coating deposition Raman spectroscopy of proteinogenic amino acids compared with their solution and crystalline state
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F17%3A10366915" target="_blank" >RIV/00216208:11320/17:10366915 - isvavai.cz</a>
Výsledek na webu
<a href="http://dx.doi.org/10.1016/j.saa.2017.05.043" target="_blank" >http://dx.doi.org/10.1016/j.saa.2017.05.043</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.saa.2017.05.043" target="_blank" >10.1016/j.saa.2017.05.043</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Drop coating deposition Raman spectroscopy of proteinogenic amino acids compared with their solution and crystalline state
Popis výsledku v původním jazyce
The Raman spectra of 20 proteinogenic amino acids were recorded in the solution, glass phase (as drop coating deposition Raman (DCDR) samples) and crystalline forms in the wide spectral range of 200-3200 cm(-1). The most apparent spectral differences between the Raman spectra of the crystalline forms, glass phases and aqueous solutions of amino acids were briefly discussed and described in the frame of published works. The possible density dependencies of spectral bands were noted. In some cases, a strong influence of the sample density, as well as of the organization of the water envelope, was observed. The most apparent changes were observed for Ser and Thr. Nevertheless, for the majority of amino acids, the DCDR sample form is an intermediate between the solution and crystalline forms. In contrast, aromatic amino acids have only a small sensitivity to the form of the sample. Our reference set of Raman spectra is useful for revealing discrepancies between the SERS and solid/solution spectra of amino acids. We also found that some previously published Raman spectra of polycrystalline samples resemble glassy state rather than crystalline spectra. Therefore, this reference set of spectra will find application in every branch of Raman spectroscopy where the spectra of biomolecules are collected from coatings.
Název v anglickém jazyce
Drop coating deposition Raman spectroscopy of proteinogenic amino acids compared with their solution and crystalline state
Popis výsledku anglicky
The Raman spectra of 20 proteinogenic amino acids were recorded in the solution, glass phase (as drop coating deposition Raman (DCDR) samples) and crystalline forms in the wide spectral range of 200-3200 cm(-1). The most apparent spectral differences between the Raman spectra of the crystalline forms, glass phases and aqueous solutions of amino acids were briefly discussed and described in the frame of published works. The possible density dependencies of spectral bands were noted. In some cases, a strong influence of the sample density, as well as of the organization of the water envelope, was observed. The most apparent changes were observed for Ser and Thr. Nevertheless, for the majority of amino acids, the DCDR sample form is an intermediate between the solution and crystalline forms. In contrast, aromatic amino acids have only a small sensitivity to the form of the sample. Our reference set of Raman spectra is useful for revealing discrepancies between the SERS and solid/solution spectra of amino acids. We also found that some previously published Raman spectra of polycrystalline samples resemble glassy state rather than crystalline spectra. Therefore, this reference set of spectra will find application in every branch of Raman spectroscopy where the spectra of biomolecules are collected from coatings.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10610 - Biophysics
Návaznosti výsledku
Projekt
<a href="/cs/project/GBP205%2F12%2FG118" target="_blank" >GBP205/12/G118: Nanobiofotonika pro medicínu budoucnosti</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2017
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
ISSN
1386-1425
e-ISSN
—
Svazek periodika
185
Číslo periodika v rámci svazku
5 October
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
10
Strana od-do
207-216
Kód UT WoS článku
000405251700028
EID výsledku v databázi Scopus
2-s2.0-85020007300