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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