The entry of the human immunodeficiency virus type 1 (HIV-1) into target cells requires the interaction of viral envelope glycoprotein, gp120, with the human CD4 glycoprotein and a chemokine receptor, usually CCR5 or CXCR4. The natural ligand for CXCR4 is the chemokine SDF-1 that inhibits entry and replication of X4 HIV-1 strains. SDF-1 is produced in two forms, SDF-1α (68 residues) and SDF-1β (72 residues); the difference between them lies in the additional four C-terminal amino acids in the SDF-1β sequence. Despite the relevance of the N-terminal site in determining the SDF anti HIV-1 activity, SDF-1β has a stronger activity than SDF-1α. Here we demonstrate that a synthetic peptide mapped on the C-terminus of SDF-1β presents inhibitory activity, whereas an analogue reproducing the C-terminal trait of SDF-1α does not show any activity. The opposite biological effect of the two peptides correlates with the type of interaction they each have with heparin and chondroitin sulfate.
ASJC Scopus subject areas
- Organic Chemistry