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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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