title: Two interaction modes of the gp41-derived peptides with gp41 and their correlation with antimembrane fusion activity.
abstract: Peptides derived from gp41 effectively block the gp41-mediated cell fusion or HIV infection. A 36-mer (naDP178), 51-mer (C51) and 27-mer peptide (C27) from the membrane proximal region of gp41 have been examined their interaction modes with the coiled-coil motif of gp41 presented in thioredoxin (Trx-N) or the bacterially expressed ectodomain of gp41 (Ec-gp41ec). All of these peptides effectively inhibited the gp41-mediated membrane fusion, however, they showed distinct interaction modes with Ec-gp41ec or Trx-N. C51 peptide bound tightly to Trx-N, and it increased the solubility of Ec-gp41ec. naDP178 showed very weak binding affinity to Trx-N, however, it effectively solubilized Ec-gp41ec. In contrast, C27 peptide showed significant binding to Trx-N; however, it did not affect the solubility of Ec-gp41ec. These interaction modes of C-peptides were assumed to be related to their different inhibitory mechanism against gp41-mediated cell fusion.
authors.affiliation: Structural Biology Center, Bioanalysis and Biotransformation Research Center, Medicinal Chemistry Research Center, Korea Institute of Science and Technology, PO Box 131, Cheongryang, Seoul, 130-650, Korea.
authors.forename: J R
authors.initials: JR
authors.lastname: Ryu
authors.forename: B S
authors.initials: BS
authors.lastname: Jin
authors.forename: M J
authors.initials: MJ
authors.lastname: Suh
authors.forename: Y S
authors.initials: YS
authors.lastname: Yoo
authors.forename: S H
authors.initials: SH
authors.lastname: Yoon
authors.forename: E R
authors.initials: ER
authors.lastname: Woo
authors.forename: Y G
authors.initials: YG
authors.lastname: Yu
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001665:Binding Sites; D004926:Escherichia coli / Q000235:genetics; D015700:HIV Envelope Protein gp41 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015658:HIV Infections / Q000209:etiology* / Q000378:metabolism / Q000821:virology; D015497:HIV-1 / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity*; D006801:Humans; D008561:Membrane Fusion / Q000502:physiology*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012995:Solubility; D013879:Thioredoxins / Q000378:metabolism
chemical_list: D015700:HIV Envelope Protein gp41; D010446:Peptide Fragments; D011994:Recombinant Proteins; D013879:Thioredoxins