Binding Sites for Luminescent Amyloid Biomarkers from non-Biased Molecular Dynamics Simulations

Autor:	König, Carolin, Skånberg, Robin, Hotz, Ingrid, Ynnerman, Anders, Norman, Patrick, Linares, Mathieu
Rok vydání:	2018
Předmět:	Physics - Chemical Physics Physics - Biological Physics Quantitative Biology - Biomolecules
Zdroj:	Chem. Commun., 2018,54, 3030-3033
Druh dokumentu:	Working Paper
DOI:	10.1039/C8CC00105G
Popis:	A very stable binding site for the interaction between an pentameric oligothiophene and an amyloid-$\beta$(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 1,200 kJ/mol due to the interactions between the anionic carboxyl groups of the probe and the cationic $\epsilon$-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. Comment: not peer-reviewed pre-print
Databáze:	arXiv
Externí odkaz:	http://arxiv.org/abs/1808.07552 Zobrazit plný text záznamu View this record from Arxiv