Skip to Content
Report an accessibility problem
Giovanna Ghirlanda

Giovanna Ghirlanda

Professor, School of Molecular Sciences, College of Liberal Arts and Sciences

Giovanna.Ghirlanda@asu.edu

480-965-6645

School of Molecular Science
Arizona State University
PO Box 871604
Tempe, AZ 85287-1604

Titles

  • Professor, School of Molecular Sciences, College of Liberal Arts and Sciences

Biography

Giovanna Ghirlanda is a professor of chemistry at Arizona State University. Her research interests are in chemical biology, protein chemistry, and protein engineering. Professor Ghirlanda received a BSc/MSc degree in Medicinal Chemistry and a PhD in Organic Chemistry from the University of Padova, Italy, with a thesis on the redox catalytic properties of supramolecular metallocomplexes.

Prior to joining ASU, she pursued postdoctoral work at the University of Pennsylvania with Professor William F. DeGrado (now at the University of California San Francisco), specializing on de novo design of peptides and proteins. Her research is in the area of chemical biology and focuses on the design of functional proteins. A major thrust is in the area of sustainable fuel production, designing protein-based hybrid metalloenzymes that catalyze hydrogen production and carbon dioxide reduction in mild conditions. Other projects in the lab include the design of antiviral lectins and work on protein folding in WW domains, in collaboration with Professor Banu Ozkan (Physics, ASU).

Education

  • PhD, Organic Chemistry, University of Padova, 1996
  • BSc/MSc, Medicinal Chemistry, University of Padova, 1991

Journal Articles

2014

Flory, J. D., T. Johnson, C. R. Simmons, S. Lin, G. Ghirlanda and P. Fromme. 2014. Purification and assembly of thermostable Cy5 labeled γ-PNAs into a 3D DNA nanocage. Artificial DNA: PNA & XNA 5(3):e992181. DOI: 10.4161/1949095X.2014.992181. (link )

2013

Flory, J. D., S. Shinde, S. Lin, Y. Liu, G. Ghirlanda and P. Fromme. 2013. PNA-peptide assembly in a 3D DNA nanocage at room temperature. Journal of the American Chemical Society 135(18):6985-6993. DOI: 10.1021/ja400762c. (link )