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SERS analysis of saliva and its key components: The effects of various collection methods, sample dilution, excitation wavelengths, and enhancing substrates

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F25%3A43933230" target="_blank" >RIV/60461373:22340/25:43933230 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/pii/S0924203125000219" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0924203125000219</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.vibspec.2025.103787" target="_blank" >10.1016/j.vibspec.2025.103787</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    SERS analysis of saliva and its key components: The effects of various collection methods, sample dilution, excitation wavelengths, and enhancing substrates

  • Original language description

    Recently, human saliva has become a subject of research as an excellent material for patient-friendly diagnostics. An increasing number of diagnostic tests utilize saliva due to its easy and noninvasive collection, eliminating the patient&apos;s stress. Simultaneously, developing Surface-Enhanced Raman Scattering (SERS) spectroscopy offers new possibilities for analyzing saliva&apos;s composition. Saliva is a complex biological material; many factors influence its composition, including medication use, diseases, stress, hormone levels, diet, age, and hydration. This complexity raises the question of whether it is possible to observe and definitively attribute changes in specific substances through SERS spectra. One of the key questions we posed is how the SERS spectrum will change with an increased level of alpha-amylase 1 A (AMY1A), an enzyme marker of acute stress. AMY1A forms complexes with proline-rich proteins (PRP). Thus, we examined whether similar spectral changes are observed with a PRP level increase in saliva. Another focus was lysozyme C (LYZ C), a nonspecific marker of infectious diseases. We examined how increased levels of LYZ C affect SERS spectra, particularly considering its sensitivity to changes in the ionic composition of saliva and its complexation with PRP and lactoferrin (LF). Moreover, we explored whether the albumin (HSA) level, which plays a vital role in regulating osmotic pressure, influences LYZ C activity and how it is manifested in SERS. Furthermore, we investigated the effect of saliva dilution and collection methods on SERS spectra. We searched for correlations with significant components such as AMY1A, HSA, LYZ C, LF, and Poly-L-proline (PLP is an analog of PRP). We showed the role of gold (Au) and silver (Ag) substrates, comparing the spectral differences. Solving the issues is crucial for the ability of SERS techniques to detect and/ or monitor biomolecules in saliva and can lead to significant advancements in noninvasive diagnostics.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10400 - Chemical sciences

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2025

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    VIBRATIONAL SPECTROSCOPY

  • ISSN

    0924-2031

  • e-ISSN

    1873-3697

  • Volume of the periodical

    138

  • Issue of the periodical within the volume

    May

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    15

  • Pages from-to

    103787

  • UT code for WoS article

    001448118000001

  • EID of the result in the Scopus database

    2-s2.0-86000627964