Alessandra Astegno

Biography

Dr. A. Astegno is interested in many aspects of protein chemistry, including folding, evolution and structure-function relationship of proteins and macromolecular assemblies. In particular, she has a solid background in recombinant protein expression and purification, functional and structural characterization of PLP-dependent enzymes as well as metallo-proteins. PLP dependent enzymes have been studied in both pathogens as possible targets for the design and development of therapeutic agents (CS lyase from Corynebacterium diphtheriae and ornithine aminotransferase from Toxoplasma gondii) and higher plants (glutamic acid decarboxylase from Arabidopsis thaliana) as an example of specialization during phylogenetic evolution when the kingdoms diverged. More recently, the work of Dr. Astegno focused on the study of calcium signaling in higher plants through biochemical and biophysical characterization of calcium sensor proteins, such as calmodulin 1 of Arabidopsis thaliana. Dr. Astegno also participated in the structural and functional characterization of non-symbiotic hemoglobins of higher plants (AHb1 and AHb2 of Arabidopsis thaliana) in order to correlate their chemical reactivity to physiological function

Research Interest

kinetic studies (steady state and pre-steady state kinetics); ï‚· reaction mechanism studies (substrate specificity, chemical modification and site-directed mutagenesis); ï‚· protein-protein and protein-ion interactions (isothermal titration calorimetry, fluorescence and absorption spectroscopy, circular dichroism, dynamic light scattering); ï‚· cofactor reactivity and protein stability on heating and denaturing agents (differential scanning calorimetry, limited proteolysis); ï‚· protein engineering; ï‚· structural studies (size exclusion chromatography, native page).