- Tytuł:
- Probing of Cu2+ ions binding to A β (5−16) peptide using ITC measurements and MD simulations
- Autorzy:
-
Makowska, J.
Żmudzińska, W.
Wyrzykowski, D.
Brzozowski, K.
Zblewska, H.
Chmurzyński, L. - Powiązania:
- https://bibliotekanauki.pl/articles/1938620.pdf
- Data publikacji:
- 2016
- Wydawca:
- Politechnika Gdańska
- Tematy:
-
A β (5 − 16) fragments
metal-peptide binding
isothermal titration calorimetry
molecular dynamics simulations - Opis:
- It is shown that probably three residues: His6, His14 and His16 in the original sequence A β (1−42) serve as metal-binding sites for Cu2+ions. On the other hand, there is a possibility that only one of them plays a crucial role in the formation of the{A β (1-42)-Cu2+} complex. The isothermal titration calorimetry (ITC) measurements supported by molecular dynamic simulation (MD) with the NMR-derived restrains were used to investigate the interactions of Cu2+ with A β(5-16), a fragment of the A β(1-42) protein, with the following sequence: Ac-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-NH2, termed HZ1. The conditional thermodynamic parameters suggest that the formation of the Cu2+-HZ1 complex is both an enthalpy and entropy driven process under the experimental conditions. The studies presented here (after comparison with our previous results) show that the affinity of peptides to copper metal ions depends on two factors: the primary structure (amino acid composition) and the shape of the peptide conformation adopted.
- Źródło:
-
TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk; 2016, 20, 4; 409-416
1428-6394 - Pojawia się w:
- TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk
- Dostawca treści:
- Biblioteka Nauki
Artykuł