Download Full Text (232 KB)

Download Abstract (8 KB)

Download Description Sheet (812 KB)

Download Protein Modeling Powerpoint (3.0 MB)

Download Presentation (31.7 MB)

Download Poster (2.1 MB)

Submission Date

Fall 2021


Sickle cell anemia is a hematologic disorder impacting over 15 million people worldwide. It is caused by a single point mutation in the gene hemoglobin-Betha, where a glu group is replaced by val (GAG --- GTG) in the seventh codon (glu7val) of chromosome 1. In this study, we are comparing the anti-sickling properties of drugs in varied conditions in order to create a drug that is effective in an O2-independent manner and with a 1:1 stoichiometry for lower dosage purposes. We used Pymol and Jmol to compare the structures of the aldehydes GBT-440 and VZHE-039, which interact on the same binding site to treat sickle cell disease. GBT-440’s bulkiness allows it to have a 1:1 stoichiometry, while VZHE-039’s solubility is due to its interaction with the hemoglobin’s alpha cleft, allowing it to be O2-independent. We identified the pyridine and pyrazole structure from GBT-440 and the methyl hydroxy moite from VZHE-039 as key structures, and created a hypothetical new drug, a hybrid of VZHE-039 and GBT-440. The pose predicted would allow the drug to interact with the sickled hemoglobin in a 1 to 1 ratio and in an O2-independent manner.

Abstract Sickle Cell.docx (8 kB)

Sickle cell Description sheet.docx (812 kB)
Description Sheet

Protein Modeling Powerpoint.pptx (3059 kB)
Protein Modeling Powerpoint

Recording .mp4 (32411 kB)

Sickle cell anemia- Poster.pptx (2111 kB)

Investigating the Structure of Potential New Drug to Treat Sickle Cell Anemia through Inhibition of the Polymerization of Hemoglobin S​