Abstract
The halovirs are linear, lipophilic peptides produced by a marine-derived fungus of the genus Scytalidium. We recently reported that these molecules possess potent in vitro activity against the herpes simplex viruses 1 and 2. Here we present structure-activity relationships defining key structural elements for optimal viral inhibition. Results demonstrate that an N(alpha)-acyl chain of at least 14 carbons and an Aib-Pro dipeptide are critical for maintaining the antiviral activity.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antiviral Agents / chemical synthesis*
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Antiviral Agents / pharmacology
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Biological Products / chemical synthesis*
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Biological Products / pharmacology
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Chlorocebus aethiops
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Fungal Proteins / chemical synthesis*
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Fungal Proteins / pharmacology
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Herpesvirus 1, Human / drug effects
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Herpesvirus 1, Human / physiology
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Oligopeptides / chemical synthesis*
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Oligopeptides / pharmacology
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Structure-Activity Relationship
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Vero Cells
Substances
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Antiviral Agents
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Biological Products
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Fungal Proteins
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Oligopeptides
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halovir A