NDA@SZTAKI

Interaction of anticancer reduced Schiff base coumarin derivatives with human serum albumin investigated by fluorescence quenching and molecular modeling

DĂśmĂśtĂśr, Orsolya

Tuccinardi, Tiziano

Karcz, Darius

Enyedy, Éva Anna

Elsevier

2014

QD Chemistry / kĂŠmia

The specific binding of five reduced Schiff base derived 7-amino-coumarin compounds with
antitumor activity to human serum albumin, the principal binding protein of blood, was
studied by fluorescence spectroscopy. Their conditional binding constants were computed and
the reversible binding at the Sudlow’s site I was found to be strong (KD ~ 0.03-2.09 M).
Based on the data albumin can provide a depot for the compounds and is responsible for their
biodistribution and transport processes. The experimental data is complemented by protein–
ligand docking calculations for two representatives which support the observations. The
proton dissociation constants of the compounds were also determined by UV-Vis
spectrophotometric and fluorometric titrations to obtain the actual charges and distribution of
the species in the various protonation states at physiological pH.

angol

Article

PeerReviewed

info:eu-repo/semantics/article

text

http://real.mtak.hu/7143/1/Bioorg_Domotor.pdf

Dömötör, Orsolya and Tuccinardi, Tiziano and Karcz, Darius and Enyedy, Éva Anna (2014) Interaction of anticancer reduced Schiff base coumarin derivatives with human serum albumin investigated by fluorescence quenching and molecular modeling. BIOORGANIC CHEMISTRY, 52. pp. 16-23. ISSN 0045-2068

http://real.mtak.hu/7143/

doi:10.1016/j.bioorg.2013.10.003