Collection of personal information
Your personal information is collected under
the authority of section 33(c) of the Freedom of Information and Protection of Privacy Act. If
you have any questions about the collection or use of this information, please visit our
Access to Information page.
Farideh Jalilehvand, PhD
PhD in Physical Inorganic Chemistry Royal Institute of Technology (KTH)/ SWEDENPhD in Inorganic Chemistry Ochanomizu University / Japan
Areas of Research
Heavy Metal Complex Formation with Amino Acids
Accumulation of heavy metal ions in the environment causes adverse health effects. “Soft” metal ions have a high affinity for thiol (-SH) groups, in e.g., amino acid L-cysteine, the cysteine-rich protein metallothionein, and tripeptide glutathione, which is the most abundant cellular thiol in the body and has important in vivo functions for protection against heavy metal ions. Uptake via food, drinking water and air of Hg(II), Pb(II) and Cd(II) can affect human metabolism by blocking enzymatic functions. Thiol-containing drugs, e.g. D-penicillamine (3,3´-dimethylcysteine), are clinically used for heavy metal detoxification. Similarly, metal based antitumor active complexes may interact with thiol-containing proteins, which could render their activities. We have applied a novel combination of different spectroscopic methods such as multi-nuclear NMR, EXAFS and vibrational spectroscopy for investigating the coordination of such metal ions to glutathione, cysteine and its derivatives, to elucidate the structure of their complexes, and to evaluate the distribution of these species in aqueous solution. The information on structure and bonding of heavy metal complexes with such thiol-containing small molecules can assist us to design new chelating agents/ drugs with improved efficiency for detoxification by increasing their bonding efficiency.
Accumulation of heavy metal ions in the environment causes adverse health effects. “Soft” metal ions have a high affinity for thiol (-SH) groups, in e.g., amino acid L-cysteine, the cysteine-rich protein metallothionein, and tripeptide glutathione, which is the most abundant cellular thiol in the body and has important in vivo functions for protection against heavy metal ions. Uptake via food, drinking water and air of Hg(II), Pb(II) and Cd(II) can affect human metabolism by blocking enzymatic functions. Thiol-containing drugs, e.g. D-penicillamine (3,3´-dimethylcysteine), are clinically used for heavy metal detoxification. Similarly, metal based antitumor active complexes may interact with thiol-containing proteins, which could render their activities. We have applied a novel combination of different spectroscopic methods such as multi-nuclear NMR, EXAFS and vibrational spectroscopy for investigating the coordination of such metal ions to glutathione, cysteine and its derivatives, to elucidate the structure of their complexes, and to evaluate the distribution of these species in aqueous solution. The information on structure and bonding of heavy metal complexes with such thiol-containing small molecules can assist us to design new chelating agents/ drugs with improved efficiency for detoxification by increasing their bonding efficiency.
Supervising degrees
Chemistry - Doctoral: Accepting Inquiries
Chemistry - Masters: Accepting Inquiries
More information
Working with this supervisor
Chemistry graduates with strong background in Inorganic Chemistry and Spectroscopy are encouraged to apply.
Contact this supervisor
Complete the following form if you are interested in working with this supervisor for your Graduate Program. All fields are required, unless indicated otherwise.