Ks. Ryu et al., INTERACTION OF GLUCAGON WITH DIMYRISTOYLPHOSPHATIDYLCHOLINE IN VESICULAR AND DISCOIDAL COMPLEXES, Journal of Biochemistry, 123(1), 1998, pp. 55-61
Glucagon fragments dimyristoylphosphatidylcholine liposomes into disco
idal complex under appropriate conditions, The concentration of glucag
on required to fragment the vesicles increases with increasing pH, whi
ch appears to be related to the glucagon binding, It was also observed
that the fragmentation is facilitated by NaCl, which is also due to i
ncreased glucagon binding, From the quenching of Trp fluorescence by d
oxyl group located at various positions of the acyl chain of the lipid
, Trp of glucagon was found to be located close to the bilayer surface
in the vesicular complex, However, the Trp fluorescence was quenched
by the doxyl group in the discoidal complex to an equal extent regardl
ess of the position of this spin label in the acyl chain, This and the
results of second derivative UV spectroscopy of Tyr suggested that se
gments including Tyr-13 and Trp-25 are involved in the discoidal compl
ex formation and that the orientation of glucagon is not normal to the
bilayer surface.