Presentation Title

Regulating Sodium Ion Concentrations: Investigation of a Class of Potential Peptide Therapeutics

Location

Room 2903

Session Format

Poster Presentation

Research Area Topic:

Natural & Physical Sciences - Chemistry

Abstract

Regulation of ion concentrations in aqueous solutions is critical in biochemistry research due to the effects of ions on protein structures. Proteins and peptides are stabilized by non-covalent interactions which may be disrupted by changes in the ionic content of solutions. These changes may result in a destabilization of the native conformation of a given protein, thereby preventing its typical function. A well-studied peptide known to be soluble and highly structured in aqueous solutions was determined to be insoluble in aqueous solutions from a local water source. Subsequent studies of this peptide and other proteins indicate that ion concentrations in this water affect multiple peptide and protein structures. Analysis of various water samples via ICP-MS indicate that high sodium ion concentrations in the water are the most likely cause of these anomalies in protein structure and function. Quantum chemical computations on model systems also provide evidence that sodium ions can disrupt stabilizing cation-pi interactions in this particular peptide, likely causing it to unfold. These initial data suggest that excess sodium ions and other metal ions may interfere with a variety of intermolecular forces within proteins. Circular dichroism experiments also give insight into the structural effects of high sodium ion concentrations in peptides and proteins. Characterization of another protein provides additional data indicating that sodium ions interfere with helical structure in collagen. Collagens triple helix is eliminated when placed in aqueous solution with high sodium ion concentrations. Removal of excess ions via a desalting method regenerates the characteristic triple helix. Taken together, these results indicate the negative impacts of excess sodium ions in protein structure and function. Additional circular dichroism experiments and binding studies to assay the effects of specific sodium ion concentrations on various proteins and peptides will be completed. The potential for peptides to bind sodium with high affinity will also be investigated. While protein precipitation via high salt concentrations is a standard purification protocol in biochemistry, these results demonstrate the significance of water quality and ionic content during all experimentation and point to broader implications in protein and peptide biochemistry and therapeutics. The latest results from these studies and the potential for this class of peptides to be tuned as therapeutics in the removal of excess sodium ion will be reported.

Presentation Type and Release Option

Presentation (Open Access)

Start Date

4-16-2016 1:30 PM

End Date

4-16-2016 2:30 PM

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Apr 16th, 1:30 PM Apr 16th, 2:30 PM

Regulating Sodium Ion Concentrations: Investigation of a Class of Potential Peptide Therapeutics

Room 2903

Regulation of ion concentrations in aqueous solutions is critical in biochemistry research due to the effects of ions on protein structures. Proteins and peptides are stabilized by non-covalent interactions which may be disrupted by changes in the ionic content of solutions. These changes may result in a destabilization of the native conformation of a given protein, thereby preventing its typical function. A well-studied peptide known to be soluble and highly structured in aqueous solutions was determined to be insoluble in aqueous solutions from a local water source. Subsequent studies of this peptide and other proteins indicate that ion concentrations in this water affect multiple peptide and protein structures. Analysis of various water samples via ICP-MS indicate that high sodium ion concentrations in the water are the most likely cause of these anomalies in protein structure and function. Quantum chemical computations on model systems also provide evidence that sodium ions can disrupt stabilizing cation-pi interactions in this particular peptide, likely causing it to unfold. These initial data suggest that excess sodium ions and other metal ions may interfere with a variety of intermolecular forces within proteins. Circular dichroism experiments also give insight into the structural effects of high sodium ion concentrations in peptides and proteins. Characterization of another protein provides additional data indicating that sodium ions interfere with helical structure in collagen. Collagens triple helix is eliminated when placed in aqueous solution with high sodium ion concentrations. Removal of excess ions via a desalting method regenerates the characteristic triple helix. Taken together, these results indicate the negative impacts of excess sodium ions in protein structure and function. Additional circular dichroism experiments and binding studies to assay the effects of specific sodium ion concentrations on various proteins and peptides will be completed. The potential for peptides to bind sodium with high affinity will also be investigated. While protein precipitation via high salt concentrations is a standard purification protocol in biochemistry, these results demonstrate the significance of water quality and ionic content during all experimentation and point to broader implications in protein and peptide biochemistry and therapeutics. The latest results from these studies and the potential for this class of peptides to be tuned as therapeutics in the removal of excess sodium ion will be reported.