A Rationally Designed Synthetic Mimic of the Discontinuous CD4-Binding Site of HIV-1 gp120

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.     

Utilization of Messenger in Adenovirus-2-infected Cells at Normal and Elevated Temperatures

THE regulation of protein synthesis in eukaryotic cells appears to be distinctly different from that in prokaryotes. The long-lived messenger RNA in eukaryotes suggests that control of protein synthesis occurs partially at the level of translation and regulation at the level of initiation of translation of messenger RNA has been found under several different conditions in mammalian cells^1–6.