Mode of action of the gramicidin S analogs lacking hydrophilic amino acid residues on biomembranes.
The gramicidin S analog lacking basic ornithine residues, cyclo(-Val-Ala-Leu-delta Phe-Pro-)2 (where delta Phe represents alpha, beta-dehydrophenylalanine), increased the K+ permeability of human erythrocytes and Staphylococcus aureus similarly to the parent gramicidin S. This analog altered the normal discoid shape of human erythrocytes to an invaginated form. The direction of the shape change was opposite to the case of gramicidin S causing crenated cells. We suppose that the analog accumulated predominantly into the inner half monolayer of membrane and destabilized the membrane structure, resulting in a break in the membrane.
Katsu
T
T
Faculty of Pharmaceutical Sciences, Okayama University, Japan.
Sanchika
K
K
Takahashi
M
M
Kishimoto
Y
Y
Fujita
Y
Y
Yoshitomi
H
H
Waki
M
M
Shimohigashi
Y
Y
D000596:Amino Acids / Q000737:chemistry; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism; D006096:Gramicidin / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D066298:In Vitro Techniques; D008297:Male; D008566:Membranes / Q000187:drug effects / Q000378:metabolism; D015221:Potassium Channels / Q000187:drug effects; D013211:Staphylococcus aureus / Q000187:drug effects / Q000378:metabolism
D000596:Amino Acids; D015221:Potassium Channels; D006096:Gramicidin