On the antibacterial activity of normal and reversed magainin 2 analogs against Helicobacter pylori.
Magainin 2 is an antimicrobial peptide isolated from the skin of Xenopus laevis. We have tested the antibacterial activities of normal and reversed magainin 2 analogs against two strains of Helicobacter pylori (ATCC 43526, ATCC 43579), compared with those against Escherichia coli (ATCC 25922) and Staphylococcus aureus (ATCC 25923). Among these analogs, MSI-78A showed the strongest activity against H. pylori. The MIC (minimum inhibitory concentration) values were almost the same as those against E. coli and S. aureus. No or lesser activity was observed in all the reversed peptides compared to the corresponding normal magainin 2 analogs. Based on the CD (circular dichroism) measurement, the more active peptide tends to show a higher alpha-content. The positively-charged five amino acids (KILKK) positioned at the C terminus on the amphipathical alpha-helical structure play important roles in exerting the strong activity against H. pylori. This indicates that the net charge of the cell surface in H. pylori may be more negative than that of E. coli, though both strains belong to the same genus.
Iwahori
A
A
Sagami Chemical Research Center, Kanagawa, Japan.
Hirota
Y
Y
Sampe
R
R
Miyano
S
S
Takahashi
N
N
Sasatsu
M
M
Kondo
I
I
Numao
N
N
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides; D002942:Circular Dichroism; D004926:Escherichia coli / Q000187:drug effects; D016480:Helicobacter pylori / Q000187:drug effects*; D006461:Hemolysis / Q000187:drug effects; D006801:Humans; D054806:Magainins; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology*; D013211:Staphylococcus aureus / Q000187:drug effects; D013329:Structure-Activity Relationship; D029867:Xenopus Proteins
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D054806:Magainins; D010455:Peptides; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus