University of Kentucky

Poster Title

Screening of a Peptide Library for a Neuroprotective Binding Target

Presenter Information

Sabita Dumre, University of Kentucky

Institution

University of Kentucky

Abstract

Emerging evidence has shown that the well-known glycolytic enzyme, glyceraldehyde-3- phosphate dehydrogenase (GAPDH), interacts with numerous binding partners in the cell to perform a wide range of functions, including the mediation of cell apoptosis. The subsequent identification of small molecules that inhibit apoptosis and provide neuroprotection in cell culture and animal models, through their binding interaction with GAPDH, suggests that this protein may be a potential target for the treatment of neurodegenerative disorders. With the emergence of combinatorial library design and screening strategies, peptides provide an attractive scaffold to select individual sequences in the laboratory with desired interactions with a defined target, from a large collection of candidate sequences. In this project, we utilized phage display to screen trillions of unique peptide sequences for interactions to GAPDH. Multiple rounds of biopanning and amplification enriched the library over 10 billion-fold for binders to GAPDH. Preliminary analysis of selected peptide sequences has identified members known to interact with GAPDH, as well as novel sequences which could elucidate other cellular interactions.

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Screening of a Peptide Library for a Neuroprotective Binding Target

Emerging evidence has shown that the well-known glycolytic enzyme, glyceraldehyde-3- phosphate dehydrogenase (GAPDH), interacts with numerous binding partners in the cell to perform a wide range of functions, including the mediation of cell apoptosis. The subsequent identification of small molecules that inhibit apoptosis and provide neuroprotection in cell culture and animal models, through their binding interaction with GAPDH, suggests that this protein may be a potential target for the treatment of neurodegenerative disorders. With the emergence of combinatorial library design and screening strategies, peptides provide an attractive scaffold to select individual sequences in the laboratory with desired interactions with a defined target, from a large collection of candidate sequences. In this project, we utilized phage display to screen trillions of unique peptide sequences for interactions to GAPDH. Multiple rounds of biopanning and amplification enriched the library over 10 billion-fold for binders to GAPDH. Preliminary analysis of selected peptide sequences has identified members known to interact with GAPDH, as well as novel sequences which could elucidate other cellular interactions.