Oxidatively-mediated in silico epimerization of a highly
amyloidogenic segment in the human calcitonin hormone
(hCT(15-19))

J 2019

Oxidatively-mediated in silico epimerization of a highly amyloidogenic segment in the human calcitonin hormone (hCT(15-19))

HAMID, A.K.M., J.C. SALVATORE, K. WANG, P. MURAHARI, A. GULJAS et. al.

Základní údaje

Originální název

Oxidatively-mediated in silico epimerization of a highly amyloidogenic segment in the human calcitonin hormone (hCT(15-19))

Autoři

HAMID, A.K.M., J.C. SALVATORE, K. WANG, P. MURAHARI, A. GULJAS, A. RAGYANSZKI, Michael Christopher OWEN (124 Kanada, garant, domácí), B. JOJART, M. SZORI, I.G. CSIZMADIA, B. VISKOLCZ a B. FISER

Vydání

COMPUTATIONAL BIOLOGY AND CHEMISTRY, OXFORD, ELSEVIER SCI LTD, 2019, 1476-9271

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 1.850

Kód RIV

RIV/00216224:14740/19:00113246

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.compbiolchem.2019.04.005

UT WoS

000474314000029

Klíčová slova anglicky

DFNKF; Amyloidosis; Aggregation; Oxidative-stress; Molecular ageing; Peptide

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 31. 3. 2020 21:47, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

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.

Citovat

HAMID, A.K.M., J.C. SALVATORE, K. WANG, P. MURAHARI, A. GULJAS, A. RAGYANSZKI, Michael Christopher OWEN, B. JOJART, M. SZORI, I.G. CSIZMADIA, B. VISKOLCZ a B. FISER. Oxidatively-mediated in silico epimerization of a highly amyloidogenic segment in the human calcitonin hormone (hCT(15-19)). COMPUTATIONAL BIOLOGY AND CHEMISTRY. OXFORD: ELSEVIER SCI LTD, 2019, roč. 80, JUN, s. 259-269. ISSN 1476-9271. Dostupné z: https://dx.doi.org/10.1016/j.compbiolchem.2019.04.005.

@article{1635285,
   author = {Hamid, A.K.M. and Salvatore, J.C. and Wang, K. and Murahari, P. and Guljas, A. and Ragyanszki, A. and Owen, Michael Christopher and Jojart, B. and Szori, M. and Csizmadia, I.G. and Viskolcz, B. and Fiser, B.},
   article_location = {OXFORD},
   article_number = {JUN},
   doi = {http://dx.doi.org/10.1016/j.compbiolchem.2019.04.005},
   keywords = {DFNKF; Amyloidosis; Aggregation; Oxidative-stress; Molecular ageing; Peptide},
   language = {eng},
   issn = {1476-9271},
   journal = {COMPUTATIONAL BIOLOGY AND CHEMISTRY},
   title = {Oxidatively-mediated in silico epimerization of a highly amyloidogenic segment in the human calcitonin hormone (hCT(15-19))},
   url = {https://www.sciencedirect.com/science/article/pii/S1476927119300222?via%3Dihub},
   volume = {80},
   year = {2019}
}

TY  - JOUR
ID  - 1635285
AU  - Hamid, A.K.M. - Salvatore, J.C. - Wang, K. - Murahari, P. - Guljas, A. - Ragyanszki, A. - Owen, Michael Christopher - Jojart, B. - Szori, M. - Csizmadia, I.G. - Viskolcz, B. - Fiser, B.
PY  - 2019
TI  - Oxidatively-mediated in silico epimerization of a highly amyloidogenic segment in the human calcitonin hormone (hCT(15-19))
JF  - COMPUTATIONAL BIOLOGY AND CHEMISTRY
VL  - 80
IS  - JUN
SP  - 259-269
EP  - 259-269
PB  - ELSEVIER SCI LTD
SN  - 14769271
KW  - DFNKF
KW  - Amyloidosis
KW  - Aggregation
KW  - Oxidative-stress
KW  - Molecular ageing
KW  - Peptide
UR  - https://www.sciencedirect.com/science/article/pii/S1476927119300222?via%3Dihub
L2  - https://www.sciencedirect.com/science/article/pii/S1476927119300222?via%3Dihub
N2  - 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.
ER  -

HAMID, A.K.M., J.C. SALVATORE, K. WANG, P. MURAHARI, A. GULJAS, A. RAGYANSZKI, Michael Christopher OWEN, B. JOJART, M. SZORI, I.G. CSIZMADIA, B. VISKOLCZ a B. FISER. Oxidatively-mediated in silico epimerization of a highly amyloidogenic segment in the human calcitonin hormone (hCT(15-19)). \textit{COMPUTATIONAL BIOLOGY AND CHEMISTRY}. OXFORD: ELSEVIER SCI LTD, 2019, roč.~80, JUN, s.~259-269. ISSN~1476-9271. Dostupné z: https://dx.doi.org/10.1016/j.compbiolchem.2019.04.005.

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