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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Blumenthal, R. Jones, P. Pritsker, M. Shai, Y. |
| Description | Author Affiliation: Pritsker M ( Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, 76100 Israel.); |
| Abstract | Recent studies demonstrated that a synthetic fusion peptide of HIV-1 self-associates in phospholipid membranes and inhibits HIV-1 envelope glycoprotein-mediated cell fusion, presumably by interacting with the N-terminal domain of gp41 and forming inactive heteroaggregates [Kliger, Y., Aharoni, A., Rapaport, D., Jones, P., Blumenthal, R. & Shai, Y. (1997) J. Biol. Chem. 272, 13496-13505]. Here, we show that a synthetic all D-amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 (D-WT) of HIV-1 associates with its enantiomeric wild-type fusion (WT) peptide in the membrane and inhibits cell fusion mediated by the HIV-1 envelope glycoprotein. D-WT does not inhibit cell fusion mediated by the HIV-2 envelope glycoprotein. WT and D-WT are equally potent in inducing membrane fusion. D-WT peptide but not WT peptide is resistant to proteolytic digestion. Structural analysis showed that the CD spectra of D-WT in trifluoroethanol/water is a mirror image of that of WT, and attenuated total reflectance-fourier transform infrared spectroscopy revealed similar structures and orientation for the two enantiomers in the membrane. The results reveal that the chirality of the synthetic peptide corresponding to the HIV-1 gp41 N-terminal sequence does not play a role in liposome fusion and that the peptides' chirality is not necessarily required for peptide-peptide interaction within the membrane environment. Furthermore, studies along these lines may provide criteria to design protease-resistant therapeutic agents against HIV and other viruses. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 13 |
| Volume Number | 95 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1998-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | HIV Envelope Protein Gp41 Chemistry HIV-1 Membrane Fusion Drug Effects Peptide Fragments Pharmacology Amino Acid Sequence Cell Membrane Metabolism Circular Dichroism Gene Products, Env HIV-2 Lipid Bilayers Liposomes Molecular Sequence Data Phosphatidylglycerols Protein Binding Protein Structure, Secondary Recombinant Fusion Proteins Spectroscopy, Fourier Transform Infrared Stereoisomerism Structure-Activity Relationship Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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