Journal
JOURNAL OF RECEPTORS AND SIGNAL TRANSDUCTION
Volume 26, Issue 5-6, Pages 453-460Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/10799890600923179
Keywords
HIV-1 gp120; CD4; HIV entry inhibition; mAb b12; scaffolded peptide; protein mimicry
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Synthetic mimetics of the CD4-binding site of HIV-1 gp120 are promising candidates for HIV-1 entry inhibition, as well as immunogen candidates for the elicitation of virus-neutralizing antibodies. On the basis of the crystal structure of gp120 in complex with CD4, we have used a recently introduced strategy for the generation of structurally diverse scaffolds to design and synthesize a scaffolded peptide, in which three fragments, making up the sequentially discontinuous binding site of gp120 for CD4, are presented in a nonlinear and discontinuous fashion through a molecular scoffold, which restrains conformational flexibility. The affinities of this molecule to CD4, as well as to the broadly neutralizing antibody mAb b12, whose epitope overlaps the CD4-binding site of gp120, were determined in competitive binding assays.
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