Sulfotyrosine residues mediate human immunodeficiency type 1 (HIV-1)entry through interactions between the viral envelope glycoprotein gp120 andthe cellular co-receptor CCR5. The sulfotyrosine-binding site on gp120 is anattractive target for the development of inhibitors that can prevent HIVinfection by blocking CCR5-gp120 interactions. Sulfated antibody 412d acts as afunctional mimic of the CCR5 N-terminus, and it inhibits HIV-1 entry.  Basedon the X-ray crystal structure of the CD4-gp120-412d ternary complex, we aredeveloping entry inhibitors targeting the sulfotyrosine-binding site on gp120. Wehave rationally designed cyclic peptides targeting the sulfotyrosine-bindingsite of CD4-activated gp120 using the crystal structure and knownconformational preferences. The design, synthesis and ability to inhibit HIV-1entry of these cyclic peptides will be presented.

Rationally designed cyclic sulfopeptides for HIV-1 entry inhibition

240th National Meeting (2010)

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