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Interactions between Salmonella typhimurium lipopolysaccharide and the antimicrobial peptide, magainin 2 amide
Author(s) -
Rana Fazale R.,
Sultany Catherine M.,
Blazyk Jack
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80616-q
Subject(s) - magainin , lipopolysaccharide , chemistry , peptide , antimicrobial peptides , amide , antimicrobial , cell envelope , salmonella , biophysics , biochemistry , bacteria , escherichia coli , biology , organic chemistry , immunology , genetics , gene
Effects of magainin 2 amide on the phase behavior of Salmonella typhimurium lipopolysaccharide were characterized by FT‐IR spectroscopy. This antimicrobial cationic peptide disorders the lipopolysaccharide at molecular ratios of lipopolysaccharide to magainin greater than 4, and can induce a temperature‐dependent structural reorientation. The nature of the five phosphate groups of lipopolysaccharide was determined by 31 P NMR spectroscopy. At pH 7.4, the net charge on the phosphates is −7. Lipopolysaccharide undoubtedly plays an important role in modulating the interactions of magainin with the gram‐negative cell envelope and may act as a molecular sponge to protect the plasma membrane.