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The N‐terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers
Author(s) -
Blaustein Robert O.,
Germann William J.,
Finkelstein Alan,
DasGupta Bibhuti R.
Publication year - 1987
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(87)80562-8
Subject(s) - phospholipid , chemistry , neurotoxin , side chain , membrane , lipid bilayer , biophysics , botulinum neurotoxin , diphtheria toxin , bilayer , stereochemistry , toxin , biochemistry , biology , organic chemistry , polymer
The heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayer membranes. Channel activity is confined to the N‐terminal half of this chain; the C‐terminal half is inactive. Channel activity is stimulated by low pH (4.5–5.5) on the cis side (the side to which protein is added), neutral pH on the opposite ( trans ) side, and cis positive voltages. These findings are strikingly similar to those previously reported for analogous fragments of diphtheria and tetanus toxins.