Abstract
Cinnamomin, a new type II ribosomeinactivating protein
(RIP), was found to be able to induce the release
of calcein loaded in lecithin small unilamellar vesicles
and the fusion or aggregation of the lecithin liposomes.
Such induction could be promoted several fold
by a pH 5.0 environment, a condition similar to that in
endocytic vesicles. Lowering the pH from 7.5 to 5.0
evoked conformational changes of cinnamomin and
unmasked its hydrophobic areas, including the exposure
of 1-anilino-8-naphthalenesulfonate (1,8-ANS)
binding sites of the molecule. Some tryptophan residues
with affinity to acrylamide were demonstrated to
participate in the lipidprotein interaction. The pH dependent
fusogenicity of type II RIP might suggest its
in vivo function as a fusogen to exert its cytotoxicity.