Mr. Ehsan Amin








Ehsan Amin M.Sc.

Ahmandian Group
Institute of Biochemistry and Molecular Biology II
Heinrich Heine University
Building: 22.03
40225 Düsseldorf
Phone +49 211 81-12043
Fax +49 211 81-12043

Mini Academic CV

University degrees:

First degree or intermediate examination:

  • B.Sc. Of physics, 2006, Isfahan University, Faculty of Science. Isfahan, Iran

Second degree and/or intermediate examination:

  • M.Sc. of Biophysics, 2009, Tehran University, Institute of Biochemistry and Biophysics, Tehran, Iran


  • E. Amin, A. A. Saboury, H. Mansury-Torshizi, & A. A. Moosavi-Movahedi, Potent inhibitory effects of benzyl and p-xylidine-bis dithiocarbamate sodium salts on activities of mushroom tyrosinase. Journal of Enzyme Inhibition and Medicinal Chemistry, 2010; 25(2): 272–281
  • S. Zolghadri, A. A. Saboury, E. Amin, A. A. Moosavi-Movahedi, A Spectroscopic Study on the Interaction between Ferric Oxide Nanoparticles and Human Hemoglobin. J. Iran. Chem. Soc., Vol. 7, Suppl., July 2010, pp. S145-S153
  • E. Amin, A. A. Saboury, H. Mansury-Torshizi. Evaluation of Synthesized 1,4-Phenylene-bis and Phenyl Dithiocarbamate Sodium Salts as Mushroom Tyrosinase Inhibitors. Acta Biochemica Polonica, 2010; Vol. 57, No 3, pp 277-283

BioStruct PhD project

Structure, function and regulation of Rho effector proteins
The GTP-binding proteins of the Rho-family (or Rho-GTPases) regulate a spectrum of functionally diverse downstream effectors and thus initiate a variety of cellular processes, ranging from cytoskeletal reorganization to gene transcription. Our interest in the Rho/ROCK and Rho/PKN interactions as targets for therapeutic and pharmaceutic interventions comes from the observation on their involvement in tumor invasion and in cardiovascular diseases. A central question of this project is to understand the molecular mechanism of the RhoA-mediated effector activation. To gain insight into the RhoA interaction with its effectors we have characterized different Rho-binding domain these effectors. Our findings support the notion of multiple effector binding sites in RhoA and strongly indicate the existence of a cooperative binding mechanism for ROCK that may be the molecular basis of Rho-mediated effector activation. To corroborate this working hypothesis we will study RhoA interaction via biophysical, biochemical, X-ray crystallographic techniques. The full length proteins we will produce and purify using a Baculovirus/Insect cell expression system.


Topic Supervisor:

undefinedPD Dr. Mohammad Reza Ahmadian, Institute for Biochemistry and Molecular Biology II, Heinrich Heine University Duesseldorf, Ahmandian Group

Complementary Supervisor:

undefinedProf. Dr.Georg Groth, Institute for Plant Biochemistry, Heinrich Heine University Duesseldorf, Groth Group

Responsible for the content: E-MailBioStruct Office