Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 3030-3033 |
| Seitenumfang | 4 |
| Fachzeitschrift | Chemical communications |
| Jahrgang | 54 |
| Ausgabenummer | 24 |
| Frühes Online-Datum | 1 März 2018 |
| Publikationsstatus | Veröffentlicht - 25 März 2018 |
Abstract
A very stable binding site for the interaction between a pentameric oligothiophene and an amyloid-β(1-42) fibril has been identified by means of non-biased molecular dynamics simulations. In this site, the probe is locked in an all-trans conformation with a Coulombic binding energy of 1200 kJ mol -1 due to the interactions between the anionic carboxyl groups of the probe and the cationic ϵ-amino groups in the lysine side chain. Upon binding, the conformationally restricted probes show a pronounced increase in molecular planarity. This is in line with the observed changes in luminescence properties that serve as the foundation for their use as biomarkers.
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- Werkstoffchemie
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in: Chemical communications, Jahrgang 54, Nr. 24, 25.03.2018, S. 3030-3033.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Binding sites for luminescent amyloid biomarkers from non-biased molecular dynamics simulations
AU - König, C.
AU - Skånberg, Robin
AU - Hotz, Ingrid
AU - Ynnerman, Anders
AU - Norman, P.
AU - Linares, Mathieu
N1 - Funding information: CK acknowledges funding by a Marie Skłodoswka-Curie International Fellowship ‘‘FreezeAlz’’ by the European Commission (Grant No. 745906). ML, RS, IH and AY thanks SeRC (Swedish e-Science Research Center) for funding. PN thanks the Swedish Research Council (Grant No. 621-2014-4646) for funding. IH thanks the strategic research environment ELLIIT for funding. The Swedish National Infrastructure for Computing (SNIC) at National Supercomputer Centre (NSC) and Center for High Performance Computing (PDC) are acknowledged for providing computer resources.
PY - 2018/3/25
Y1 - 2018/3/25
N2 - A very stable binding site for the interaction between a pentameric oligothiophene and an amyloid-β(1-42) fibril has been identified by means of non-biased molecular dynamics simulations. In this site, the probe is locked in an all-trans conformation with a Coulombic binding energy of 1200 kJ mol -1 due to the interactions between the anionic carboxyl groups of the probe and the cationic ϵ-amino groups in the lysine side chain. Upon binding, the conformationally restricted probes show a pronounced increase in molecular planarity. This is in line with the observed changes in luminescence properties that serve as the foundation for their use as biomarkers.
AB - A very stable binding site for the interaction between a pentameric oligothiophene and an amyloid-β(1-42) fibril has been identified by means of non-biased molecular dynamics simulations. In this site, the probe is locked in an all-trans conformation with a Coulombic binding energy of 1200 kJ mol -1 due to the interactions between the anionic carboxyl groups of the probe and the cationic ϵ-amino groups in the lysine side chain. Upon binding, the conformationally restricted probes show a pronounced increase in molecular planarity. This is in line with the observed changes in luminescence properties that serve as the foundation for their use as biomarkers.
UR - http://www.scopus.com/inward/record.url?scp=85044199897&partnerID=8YFLogxK
U2 - 10.48550/arXiv.1808.07552
DO - 10.48550/arXiv.1808.07552
M3 - Article
VL - 54
SP - 3030
EP - 3033
JO - Chemical communications
JF - Chemical communications
SN - 0022-4936
IS - 24
ER -