Analysis of the interaction of tumor-inhibiting compounds with serum proteins by X-ray crystallography

Structural investigation of two promising tumor-inhibiting compounds relating to their interaction with putative transporter macromolecules by X-ray crystallography. Clinical studies revealed that both drugs of interest exert a strong antiproliferative action, but the exact mode of action and especially transport mechanism is still elusive.  It is suggested that both compounds bind to serum proteins, namely human transferrin (hTf) and human serum albumin (hSA), which are important for their transport and accumulation in tumor cells. It is therefore essential to elucidate the structure of drugs complexed with transporter molecules in order to elucidate the binding sites and mechanism. The method of choice is X-ray crystallography.

Financial support:

  1. FWF stand alone project P23711: "XAS Spektroskopie von tumorhemmenden Rutheniumverbindungen." 01.11.2011-31.10.2015.
  2. DFG RO 1084/7-1: "XAS-Spektroskopie von Ga-Tumor-inhi-bierenden Verbindungen in biologischen Prozessen zum Verständnis der Koordination und des Redoxzustandes in vivo." 06.12.2006–30.09.2011.