Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy

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DOIResolve DOI: http://doi.org/10.1021/bi00147a012
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TypeArticle
Journal titleBiochemistry
ISSN0006-2960
1520-4995
Volume31
Issue32
Pages72897293; # of pages: 5
AbstractThe conformational properties of the magainin family of antimicrobial peptides in aqueous solution and in model membranes have been probed by Fourier transform infrared spectroscopy. The magainins were found to be structureless in aqueous solution at neutral pD, confirming other studies by Raman and circular dichroism spectroscopy. Increasing the pD to 10 induced the formation of predominantly a-helical secondary structures, with some & sheet. In the presence of negatively charged liposomes (dimyristoylphosphatidylglycrol), the peptides folded into a-helical secondary structures with some 8-sheet structure evident. On the other hand, in the presence of zwitterionic phospholipids (dimyristoylphosphatidylcholine), the spectra were identical to those in aqueous solution. For some magainins, the interaction with charged liposomes was modulated by the presence of cholesterol; cholesterol was found to promote the formation of 8-sheet structures, as evidenced by the appearance of amide I bands at 1614 and 1637 cm-l. Differences in structure were observed between the amidated and nonamidated forms of some peptides. From the data, a mechanism of antimicrobial action of the magainin family of peptides is proposed.
Publication date
PublisherAmerican Chemical Society
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Biodiagnostics
Peer reviewedYes
NRC number46
NPARC number9742840
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Record identifierfe05ff04-5bdb-4e66-b656-581e368734c5
Record created2009-07-17
Record modified2016-12-12
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