Benoit Smagghe Email & Phone Number

Greater Boston Area

Cancer therapeutics: Development of anti-cancer therapeutics that block the dimerization (activation) of the membrane receptor MUC1*. Development of cell based assays to determine the effect of anti-cancer therapeutics on growth rate of several types of cancers. Efficacy and toxicity studies in animals. Design, expression and purification of several engineered proteins of interest.Stem cells: Development of a xeno-free chemically defined media for the culture of embryonic stem cells and induced pluripotent stem cells. Expression and purification of a unique growth factor (NM23) that maintains its oligomerization state as a dimer, which is the only active form able to dimerize and activate the membrane receptor MUC1*. Development of a xeno-free surface that supports stem cells growth.

Greater Boston Area

Mechanisms and dynamics of integrin activation: function of the b-knee loop in the I-EGF2 domain of β3 subunit has been studied. Ligand and antibody binding (purified from hybridoma) to protein transiently expressed on mammalian cell surface (HEK 293 T) has been measured by flow cytometry Common molecular biology methods (site directed mutagenesis, overlap PCR) have been used to engineer various constructs and test them for binding. Characterization of the bent/inactive and extended/active conformational states and study of the extension kinetics. Soluble proteins have been expressed in mammalian cells (HEK 293 T, CHO LEC) and purified by standard chromatographic techniques (affinity, ion exchange and gel filtration chromatography, AKTA purifier) and analyzed by SAXS (small angle X-ray scattering):Structural study of av integrins: constructs of avb6 integrin have been designed and expressed to solve its crystal structure.

Biophysical and Biochemical Characterization of Hexacoordinate Hemoglobins: stopped-flow and flash photolysis experiments were used for the development of a new kinetic model, for the study of new hemoglobins and for the study of the role of specific amino acids on ligand binding (O2 and CO) and hexacoordination. In addition to in vitro analysis of nitric oxide reactions with both oxidation states of different hexacoordinate hemoglobin, their in vivo enzymatic activity (NO dioxygenase) was also analyzed in Escherichia coli with flavohemoglobin knock-out background. The quaternary structure of a plant non-symbiotic hemoglobin was solved using X-ray crystallography methods. All recombinant proteins were expressed in Escherichia coli and purified using standard chromatographic procedures (affinity and gel filtration chromatography).

Optimization of hybridization in situ techniques: localization of a non-symbiotic hemoglobin in leafs of the Cichorium hybrid ‘474’In situ hybridization and immunolocalisation of Cichorium hybrids ‘474’ non-symbiotic hemoglobins on semi thin section of leaves treated for induction of somatic embryogenesis. Spatial and temporal localization of hemoglobins mRNA and protein was analyzed.

Phd, Biochemistry, Biophysics And Molecular Biology

Master'S Degree, Enzyme Engineering, Bioconversion And Microbiology

Bachelor'S Degree, Cell Biology And Physiology