Document 0342
 DOCN  M9590342
 TI    How do peptide inhibitors of viral fusion work?
 DT    9509
 AU    Curtain CC; Whittaker RG; Kirkpatrick A; Waring AJ; Gordon LM; Mobley
       PW; Department of Physics, Monash University, Clayton, Victoria.
 SO    Annu Conf Australas Soc HIV Med. 1994 Nov 3-6;6:155 (unnumbered
       abstract). Unique Identifier : AIDSLINE ASHM6/95291757
 AB    It is well known that the membrane fusion process whereby viruses with
       lipid envelopes, such as HIV and related retroviruses, enter their
       target cell may be inhibited by oligopeptides with sequences homologous
       to those found in the fusion domain of the viral transenvelope protein.
       In some cases, the extent of fusion inhibition is sufficient to block
       infection by viruses in culture, making the phenomenon a possible basis
       for the development of anti-viral agents. Using electron spin resonance
       spectroscopy and other biophysical techniques we have studied the
       interaction of the fusion domain of the HIV-1 gp41 transenvelope protein
       with a variety of fusion inhibitors, including peptides and modified
       peptides, in biological membranes and model membrane systems. We have
       found that the fusion domain itself is the primary target of the
       oligopeptide and related inhibitors. That is, the inhibitors are not
       merely stabilising the membrane against fusion. The significance of this
       finding is that we would expect that an agent which reacted with part of
       the fusion protein sequence would be much more specific than a membrane
       stabilising agent which would be taken up by every cell exposed to it as
       well as the relatively small number of viral target cells.
 DE    Antiviral Agents/*PHARMACOLOGY  Electron Spin Resonance Spectroscopy
       Human  HIV Envelope Protein gp41/*PHYSIOLOGY  HIV-1/*DRUG EFFECTS
       Peptides/*PHARMACOLOGY  Support, Non-U.S. Gov't  Support, U.S. Gov't,
       P.H.S.  Viral Fusion Proteins/*ANTAGONISTS & INHIB  MEETING ABSTRACT

       SOURCE: National Library of Medicine.  NOTICE: This material may be
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