Possible New Therapeutic Treatment for Sickle Cell Disease
Submission Type
Event
Expected Graduation Date
2014
Location
Center for Natural Sciences, Illinois Wesleyan University
Start Date
4-12-2014 2:00 PM
End Date
4-12-2014 4:00 PM
Disciplines
Chemistry
Abstract
There are an estimated 300,000 children born with Sickle Cell Disease annually worldwide. Though it was the first disease to be demonstrated as a genetic disorder, a viable treatment for those with the genetic disorder still eludes us. The pathology of Sickle Cell Disease results from a point mutation on chromosome 11 that results in a switching of a hydrophilic amino acid, glutamic acid, for a hydrophobic amino acid, valine. The newly added valine is expressed on the surface of the hemoglobin protein in erythrocytes or red blood cells. Valine is able to interact with and exposed hydrophobic pocket in another deoxygenated hemoglobin molecule. These interactions lead to long polymer chains of hemoglobin and distort the shape of the cell into the commonly recognized sickle shape. Recreation of physiological conditions is required to induce polymerization. Syntheses of polypeptides that bind to hemoglobin are being tested for their effectiveness in delaying the polymerization time of hemoglobin. Polymerization time is measured by time at which an increase in absorption at 700nm occurs in the UV-Vis. Peptides showing possible potential include ZSF-6, ZSF-13, and ZSF-18.
Possible New Therapeutic Treatment for Sickle Cell Disease
Center for Natural Sciences, Illinois Wesleyan University
There are an estimated 300,000 children born with Sickle Cell Disease annually worldwide. Though it was the first disease to be demonstrated as a genetic disorder, a viable treatment for those with the genetic disorder still eludes us. The pathology of Sickle Cell Disease results from a point mutation on chromosome 11 that results in a switching of a hydrophilic amino acid, glutamic acid, for a hydrophobic amino acid, valine. The newly added valine is expressed on the surface of the hemoglobin protein in erythrocytes or red blood cells. Valine is able to interact with and exposed hydrophobic pocket in another deoxygenated hemoglobin molecule. These interactions lead to long polymer chains of hemoglobin and distort the shape of the cell into the commonly recognized sickle shape. Recreation of physiological conditions is required to induce polymerization. Syntheses of polypeptides that bind to hemoglobin are being tested for their effectiveness in delaying the polymerization time of hemoglobin. Polymerization time is measured by time at which an increase in absorption at 700nm occurs in the UV-Vis. Peptides showing possible potential include ZSF-6, ZSF-13, and ZSF-18.