Oxidatively-mediated in silico epimerization of a highly amyloidogenic segment in the human calcitonin hormone (hCT(15-19))
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F19%3A00113246" target="_blank" >RIV/00216224:14740/19:00113246 - isvavai.cz</a>
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S1476927119300222?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S1476927119300222?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.compbiolchem.2019.04.005" target="_blank" >10.1016/j.compbiolchem.2019.04.005</a>
Alternative languages
Result language
angličtina
Original language name
Oxidatively-mediated in silico epimerization of a highly amyloidogenic segment in the human calcitonin hormone (hCT(15-19))
Original language description
In order to study the effects of peptide exposure to oxidative attack, we chose a model reaction in which the hydroxyl radical discretely abstracts a hydrogen atom from the alpha-carbon of each residue of a highly amyloidogenic region in the human calcitonin hormone, hCT(15-19). Based on a combined Molecular Mechanics / Quantum Mechanics approach, the extended and folded L- and D-configuration and radical intermediate hCT(15-19) peptides were optimized to obtain their compactness, secondary structure and relative thermodynamic data. The results suggest that the epimerization of residues is generally an exergonic process that can explain the cumulative nature of molecular aging. Moreover, the configurational inversion induced conformational changes can cause protein dysfunction. The epimerization of the central residue to the D-configuration induced a hairpin structure in hCT(15-19) concomitant with a possible oligomerization of human calcitonin into A beta(1-42)-like amyloid fibrils present in patients suffering from Alzheimer's disease.
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
10608 - Biochemistry and molecular biology
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
COMPUTATIONAL BIOLOGY AND CHEMISTRY
ISSN
1476-9271
e-ISSN
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Volume of the periodical
80
Issue of the periodical within the volume
JUN
Country of publishing house
GB - UNITED KINGDOM
Number of pages
11
Pages from-to
259-269
UT code for WoS article
000474314000029
EID of the result in the Scopus database
2-s2.0-85064756752