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Using circular diehroism, this study investigated the secondary structure of the influenza A M2 transmembrane domain. When reconstituted into 1,2-dioleoyl-stl-glyc~ro-3-phosphecholine liposolneS, the M2 transmembrane domain was found to adopt a predominantly a-helical secondary structure which was unaffected by both temperature and the addition of l-aminoadamantane hydrochloride. Reeonstitution into 1,2.dioleoyl-snglycero.3.phosphoglycerol liposomes resulted in a marked decrease in helical content.

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