Title
Samli, E. Farah1,2; Thompson, Eric2; and Lake, Douglas1,2
1School of Life Sciences, Arizona State University; 2Center for Innovations in Medicine, The Biodesign Institute at Arizona State University
Human immunodeficiency virus (HIV) is a retrovirus which causes AIDS. Infection from HIV can occur through the transfer of semen, vaginal fluid, blood or breast milk from an infected individual. HIV infects CD4 T helper cells and macrophages. Gp120 on the viral envelope attaches to CD4, exposing gp41, a viral glycoprotein mediates fusion of the viral envelope with the cell membrane on helper T-cells thereby initiating HIV infection. The goal of this project is to identify and characterize peptides that bind to gp120. These peptides may have therapeutic value.
Gp120 was screened on an array composed of 4000 random 20-mer peptides. Eleven gp120-binding peptide sequences were discovered from this initial screening. Four of the peptide sequences were resynthesized for confirmation of binding studies. All four peptides were confirmed as gp120-specific in a peptide-based ELISA, but 2 of the peptides show strong binding to gp120. Peptides will be linked together as homo- and heterodimers followed by re-evaluation of binding to gp120. If homo or heterodimers bind with more specificity than single peptides, they will be evaluated in HIV neutralization assays to determine if they inhibit virus production.