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Chemical and Biomolecular Engineering




EMAIL: segatori@rice.edu
PHONE: 713-348-3536

Segatori Research Group


Laura Segatori

Associate Professor in Chemical and Biomolecular Engineering 

Joint appointment in Bioengineering & Biochemistry and Cell Biology


The flexibility of the polypeptide backbone, combined with the multitude of non-covalent interactions established by amino acid side chains, allows a protein to assume a variety of three-dimensional conformations. Failures of the folding mechanisms to assist in the formation of native protein conformations results in the accumulation of dysfunctional or unstable protein structures; trace amounts of aggregates may also occur spontaneously especially during aging. Therefore, a delicate balance between two main protective strategies –- the repair of damaged proteins and their selective degradation - has evolved in all organisms. Complex interactions among molecular effectors of the chaperone and degradation systems maintain protein homeostasis in eukaryotic cells.  These are commonly referred to as protein quality control processes (QC). QC is developed to assist the folding of newly synthesized proteins and refold or degrade polypeptides that fail to attain or maintain a native structure. Its proper function is crucial in preventing the deposition of aggregation-prone, misfolded polypeptides associated with degenerative disorders, such as Alzheimer's and Parkinson diseases.

My research interests focus on the relationship between protein folding and disease, the molecular determinants of cellular protein folding, and on the development of cell protein engineering strategies to manipulate the chaperone and degradation capacity.  Specifically, we study on loss of function diseases (using patient-derived fibroblasts of lysosomal storage diseases as model system) and gain of function diseases (Parkinson’s disease). We are focusing on the development of innovative, system-level strategies based on the integration of chemical genomics and systems biology approaches aimed at identifying modulators of the proteostasis network to restore folding, cellular trafficking and activity of mutated or misfolding prone substrates. Of particular interest to our group is also the development of technologies to measure proteasomal degradation with the objective to discover endogenous cellular factors and small molecules that function as proteasome activators. Our goals are to obtain a broader understanding of the molecular mechanisms involved in cellular protein folding, and to develop methods for manipulating eukaryotic cells, which can be used for therapeutic applications. 


Dr. Segatori is an Associate Professor in Chemical and Biomolecular Engineering, teaching in areas of biomolecular and engineering and protein engineering. She received her undergraduate education (Laurea) in Industrial Biotechnology from the University of Bologna, Italy, in 2000 and a PhD in Chemical Engineering from The University of Texas at Austin, in 2005. She was a postdoctoral fellow at The Scripps Research Institute and joined the Rice faculty in 2007. She holds joint appointments in the departments of Bioengineering and Biochemistry and Cell Biology.