Presentation Title

Effects of Ions on Peptide Structure and Function

Location

Nessmith-Lane Atrium

Session Format

Poster Presentation

Research Area Topic:

Natural & Physical Sciences - Chemistry

Abstract

A protein’s function is based on its specific structure and the intermolecular forces needed to stabilize this particular conformation. When a high ionic environment is present, it can cause the protein to become unstructured and inhibit protein function. WKWK is an example of a peptide in which structure was disrupted because it is a well-structured ë_-hairpin peptide known to have a high solubility in aqueous solutions. When this peptide is placed in water; however, a precipitate is formed. Local water samples were examined using Inductively Coupled Plasma Mass Spectroscopy (ICP-MS). The ICP-MS data showed high sodium concentration in the water, WKWK dissolved best in the water with the lowest amount of sodium ion concentration. It was therefore predicted that the sodium ions are interfering with the stabilizing cation-ìÛ interaction between the tryptophan and lysine resides. A protein in this laboratory that also exhibited structural anomalies was collagen. Collagen is a protein known for its fibrous structure and its tensile strength. When analyzed via Circular Dichroism (CD), a triple helix peak is expected. However, collagen extracted from bovine tendon in the research laboratory showed a random coil peak which indicated the collagen protein is unstructured. An Amicon was used to desalt collagen and elute potential ions that were disrupting the correct structure. When the elution samples were analyzed via ICP-MS, the greatest ion content of those samples was determined to be sodium ions. Removing these excess sodium ions should return the correct triple helical structure of collagen if the sodium ions are causing the denaturation. Further experiments will be completed to determine if the Na is the cause of the protein and peptide denaturing by adding sodium ions to the correct structure of these biomolecules.

Presentation Type and Release Option

Presentation (Open Access)

Start Date

4-16-2016 10:45 AM

End Date

4-16-2016 12:00 PM

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Apr 16th, 10:45 AM Apr 16th, 12:00 PM

Effects of Ions on Peptide Structure and Function

Nessmith-Lane Atrium

A protein’s function is based on its specific structure and the intermolecular forces needed to stabilize this particular conformation. When a high ionic environment is present, it can cause the protein to become unstructured and inhibit protein function. WKWK is an example of a peptide in which structure was disrupted because it is a well-structured ë_-hairpin peptide known to have a high solubility in aqueous solutions. When this peptide is placed in water; however, a precipitate is formed. Local water samples were examined using Inductively Coupled Plasma Mass Spectroscopy (ICP-MS). The ICP-MS data showed high sodium concentration in the water, WKWK dissolved best in the water with the lowest amount of sodium ion concentration. It was therefore predicted that the sodium ions are interfering with the stabilizing cation-ìÛ interaction between the tryptophan and lysine resides. A protein in this laboratory that also exhibited structural anomalies was collagen. Collagen is a protein known for its fibrous structure and its tensile strength. When analyzed via Circular Dichroism (CD), a triple helix peak is expected. However, collagen extracted from bovine tendon in the research laboratory showed a random coil peak which indicated the collagen protein is unstructured. An Amicon was used to desalt collagen and elute potential ions that were disrupting the correct structure. When the elution samples were analyzed via ICP-MS, the greatest ion content of those samples was determined to be sodium ions. Removing these excess sodium ions should return the correct triple helical structure of collagen if the sodium ions are causing the denaturation. Further experiments will be completed to determine if the Na is the cause of the protein and peptide denaturing by adding sodium ions to the correct structure of these biomolecules.