Effective diameters of ion channels formed by homologs of the antibiotic chrysospermin.
Radii of ion channels formed in the lipid bilayer by 4 homologs of the alamethicin-like antibiotic, chrysospermin, were determined using hydrophilic nonelectrolytes. It is shown that the replacement of isovaline amino acid at position 15 of the polypeptide chain by alpha-aminoisobutyric acid results in the decrease in the channel effective radius from 1.2 +/- 0.15 to 0.94 +/- 0.1 nm and a respective 2.5-fold decrease in channel conductance.
Ternovsky
V I
VI
Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
Grigoriev
P A
PA
Berestovsky
G N
GN
Schlegel
R
R
Dornberger
K
K
Gräfe
U
U
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000900:Anti-Bacterial Agents; D000935:Antifungal Agents / Q000737:chemistry; D023181:Antimicrobial Cationic Peptides; D004553:Electric Conductivity; D007473:Ion Channels / Q000737:chemistry* / Q000648:ultrastructure; D008051:Lipid Bilayers / Q000737:chemistry; D008969:Molecular Sequence Data; D054848:Peptaibols; D010455:Peptides / Q000737:chemistry
D000900:Anti-Bacterial Agents; D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; D007473:Ion Channels; D008051:Lipid Bilayers; D054848:Peptaibols; D010455:Peptides; C096629:chrysospermin A; C096630:chrysospermin B; C096631:chrysospermin C; C096632:chrysospermin D