Membrane fusion is a key step in the virus mediated cell fusion. The vesicu
lar dispersion serves as a model system to study the membrane fusion. We em
ployed dynamic and static light scattering to study the fusion of phosphati
dylcholine vesicles in the presence of model fusion peptide fragments from
the hemagglutinin HA2 protein. The fusion-induced aggregation under the pre
sent experimental setup exhibited strong pH dependence, similar to the pare
ntal viral protein. Replacement of the glycine residue at the extreme amino
terminus by glutamic acid (G1E) abolished fusion activity. The average mol
ecular mass and diameter of vesicular dispersion obtained from static and d
ynamic light scattering measurements respectively at neutral and acidic pH
showed about three fold increase in acidic solution containing wild type fu
sion peptide. The light scattering data are consistent with lipid mixing re
sults. The present work demonstrates the utility of light scattering as a f
acile means to monitor the fusion process. (C) 2000 Elsevier Science Irelan
d Ltd. All rights reserved.