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Updated: Jul 6, 2026

A Rapid and Quantitative Fluorimetric Method for Protein-Targeting Small Molecule Drug Screening
Published on: October 16, 2015
Impact of potential blockers on Ru(III) complex binding to human serum albumin
Lilianna Trynda-Lemiesz1, Marek Luczkowski
1Faculty of Chemistry, University of Wroclaw, F. Joliot-Curie 14, Wroclaw 50-383, Poland. LTL@wchuwr.chem.uni.wroc.pl
Abstract:
The effects of aspirin, vitamin B(12) and warfarin as potential blockers of the ruthenium binding sites in HSA were investigated through UV/visible, circular dichroism (CD), fluorescence spectroscopy and the inductively coupled plasma-atomic emission spectroscopy ICP(AES). The studies on the interactions of several biologically relevant molecules with HSA have shown that drugs like aspirin or warfarin may strongly influence the interaction of serum protein with anticancer drugs. It can derive from the influence of the drug on protein conformation or binding close to binding site of anticancer drug. Aspirin, vitB(12) and warfarin bind to IIA subdomain leading to partial blocking of the ruthenium binding site in HSA.
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