title: Increased anti-HIV-1 activity of CD4 CDR3-related synthetic peptides by scrambling and further structural modifications, including D-isomerization and dimerization.
abstract: We recently showed that S1, a sequence-scrambled form of CD4 CDR3-related synthetic peptide, has more potent inhibitory activities on HIV-1 replication and HIV-1-induced syncytium formation than the original form. In this study, a series of derivatives of S1 were synthesized and their anti-HIV-1 activities were evaluated. A D-isomer was as potent as S1, and a homodimer was 10- to 18-fold more potent than S1. The increased antiviral activity of the dimer peptide was related to alpha-helix formation, as detected by circular dichroism.
authors.affiliation: Institute of Immunological Science, Hokkaido University, Sapporo, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Kumagai
authors.forename: K
authors.initials: K
authors.lastname: Tokunaga
authors.forename: M
authors.initials: M
authors.lastname: Tsutsumi
authors.forename: K
authors.initials: K
authors.lastname: Ikuta
mesh_terms: D000595:Amino Acid Sequence; D015704:CD4 Antigens / Q000737:chemistry / Q000494:pharmacology*; D002460:Cell Line; D002942:Circular Dichroism; D000939:Epitopes / Q000737:chemistry; D015726:Giant Cells / Q000473:pathology; D015497:HIV-1 / Q000187:drug effects* / Q000472:pathogenicity / Q000502:physiology; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000494:pharmacology*; D014779:Virus Replication / Q000187:drug effects
chemical_list: D015704:CD4 Antigens; D000939:Epitopes; D010446:Peptide Fragments