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The chiral proteomic analysis applied to aging collagens by LC-MS: Amino acid racemization, post-translational modifications, and sequence degradations during the aging process

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F23%3A00571992" target="_blank" >RIV/67985823:_____/23:00571992 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216275:25310/23:39920290

  • Result on the web

    <a href="https://doi.org/10.1016/j.aca.2023.341260" target="_blank" >https://doi.org/10.1016/j.aca.2023.341260</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.aca.2023.341260" target="_blank" >10.1016/j.aca.2023.341260</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The chiral proteomic analysis applied to aging collagens by LC-MS: Amino acid racemization, post-translational modifications, and sequence degradations during the aging process

  • Original language description

    Collagen is the most abundant protein in the animal and human bodies, and it is not exempt from this aging phenomenon. Some age-related changes may appear on collagen sequences, such as increased surface hydrophobicity, the appearance of post-translational modifications, and amino acids racemization. This study has shown that the protein hydrolysis under deuterium conditions is privileged to limit the natural racemization during the hydrolysis. Indeed, under the deuterium condition, the homochirality of recent collagens is preserved whose amino acids are found in their L-form. However, in aging collagen, a natural amino acid racemization was observed. These results confirmed that the % d-amino acids are progressive according to age. The collagen sequence is degraded over time, and a fifth of the sequence information is lost during aging. Post-translational modifications (PTMs) in aging collagens can be a hypothesis to explain the modification of the hydrophobicity of the protein with the decrease of hydrophilic groups and the increase of hydrophobic groups. Finally, the exact positions of d-amino acids and PTMs have been correlated and elucidated.

  • 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

    10406 - Analytical chemistry

Result continuities

  • Project

    <a href="/en/project/GA20-03899S" target="_blank" >GA20-03899S: Affinity capillary electrokinetic methods for selective analysis of biopolymers and metabolites and for study of their interactions</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2023

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Analytica Chimica Acta

  • ISSN

    0003-2670

  • e-ISSN

    1873-4324

  • Volume of the periodical

    1262

  • Issue of the periodical within the volume

    29 June

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    10

  • Pages from-to

    341260

  • UT code for WoS article

    000990072200001

  • EID of the result in the Scopus database

    2-s2.0-85153511078