Given its complexity and high rate of mortality, Human Immunodeficiency Virus (HIV) has been one of the most studied topics by researchers and clinicians since it was identified as the causative agent for AIDS. The HIV envelope glycoprotein gp120 works as a detector and a binder that detects and binds CD4, the protein receptor in the cell membrane. Upon binding to CD4, gp120 undergoes a large conformational change and exposes the binding site for co-receptor CCR5 (or CXCR4). The binding of co-receptor causes membrane fusion of the virus and the target cell, which allows viral RNA genome to enter the target cell. Previous studies have shown that sulfotyrosine (sTyr) residues within the N-termini of CCR5 receptors are essential for the binding of gp120. Our goal is to synthesize and identify sTyr-containing peptides that can effectively disrupt the interactions between gp120 and CCR5 (or CXCR4). We synthesized sTyr from tyrosine via organic synthesis, and tested genetic incorporation of sTyr into green fluorescent protein (GPF) in response to amber nonsense codon in Escherichia coli. We next examined phage display of sTyr-containing peptide by fusing its encoding gene to the pIII gene of the phage.  After further optimization of phage display system, we will construct phage library and conduct selection against HIV gp120 protein.

Identification of sulfopeptides as HIV entry inhibitors through phage display

249th National Meeting (2015)

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