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Constrained peptide immunogens show improved binding to anti-HIV-1 antibody.
2003 MAY 21 - (NewsRx.com & NewsRx.net) -- Constrained peptide immunogens showed improved binding to anti-HIV-1 antibody gp41 monoclonal antibody.
"The human immunodeficiency virus type I (HIV-1) transmembrane glycoprotein gp41 mediates viral entry through fusion of the target cellular and viral membranes. A segment of gp41 containing the sequence Glu-Leu-Asp-Lys-Trp-Ala has previously been identified as the epitope of the HIV-1 neutralizing human monoclonal antibody 2F5 (MAb 2175). The 2175 epitope is highly conserved among HIV-1 envelope glycoproteins," researchers in the United States report.
"Antibodies directed at the 2F5 epitope have neutralizing effects on a broad range of laboratory-adapted HIV-1 variants and primary isolates," said G. B. McGaughey and collaborators at Merck Research Laboratories in West Point, Pennsylvania. "Recently, a crystal structure of the epitope bound to the Fab fragment of MAb 2F5 has shown that the 2175 peptide adopts a beta-turn conformation. We have designed cyclic peptides to adopt beta-turn conformations by the incorporation of a side-chain to side-chain lactam bridge between the i and i + 4 residues containing the Asp-Lys-Trp segment."
"Synthesis of extended, nonconstrained peptides encompassing the 2F5 epitope revealed that the 13 amino acid sequence, Glu-Leu-Leu-Glu-Leu-Asp-Lys-Trp-Ala-Ser-Leu-Trp-Asn, maximized MAb 2F5 binding," reported the investigators. "Constrained analogues of this ...
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Source: HighBeam Research, Constrained peptide immunogens show improved binding to anti-HIV-1...