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- W1997197416 abstract "Antiamoebin is a 16-residue polypeptide whose crystal structure and lytic activity in membrane vesicles have recently been reported. It is a bent helical molecule and a member of the peptaibol family of antibiotics. Under conditions which produce voltage-dependent conductance activity by other members of the family, no single-channel conductance was detected for antiamoebin, and a carrier-like mechanism was put forward to account for its mode of action. We now present evidence for pore formation that is largely voltage-insensitive, with large amplitude single-channel events on top of a background conductance that may account for the previously proposed carrier-like activity. Thus, antiamoebin may be the first instance of a peptide which can function both as an ion carrier and a pore former." @default.
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- W1997197416 date "1998-12-01" @default.
- W1997197416 modified "2023-09-25" @default.
- W1997197416 title "Antiamoebin can function as a carrier or as a pore-forming peptaibol" @default.
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- W1997197416 doi "https://doi.org/10.1016/s0005-2736(98)00184-9" @default.
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