Abstract
Using circular dichroism, this study investigated the secondary structure of the influenza A M2 transmembrane domain. When reconstituted into 1,2-dioleoyl-sn-glycero-3-phosphocholine liposomes, the M2 transmembrane domain was found to adopt a predominantly alpha-helical secondary structure which was unaffected by both temperature and the addition of 1-aminoadamantane hydrochloride. Reconstitution into 1,2-dioleoyl-sn-glycero-3-phosphoglycerol liposomes resulted in a marked decrease in helical content.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amantadine
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Amino Acid Sequence
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Circular Dichroism
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Indicators and Reagents
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Influenza A virus / chemistry*
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Liposomes
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Molecular Sequence Data
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Peptides / chemical synthesis
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Peptides / chemistry
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Phosphatidylcholines
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Phosphatidylglycerols
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Protein Conformation*
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Viral Matrix Proteins / chemistry*
Substances
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Indicators and Reagents
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Liposomes
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M-protein, influenza virus
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M2 protein, Influenza A virus
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Peptides
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Phosphatidylcholines
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Phosphatidylglycerols
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Viral Matrix Proteins
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1,2-dioleoyl-sn-glycero-3-phosphoglycerol
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Amantadine
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1,2-oleoylphosphatidylcholine