Solvation dynamics of DCM is studied in DMPC vesicle in the presence of a protein, human serum albumin (HSA). In bulk water, solvation dynamics of DCM bound to HSA displays a 10 ns component. This component is absent when HSA is entrapped in the vesicle. This suggests that the protein does not undergo tumbling inside the vesicle. In the vesicle, solvation dynamics in the presence of HSA is slower compared to that in its absence. Solvation dynamics below the gel transition temperature (T-c approximate to 23degreesC) is about two times slower than that above it. (C) 2003 Elsevier B.V. All rights reserved.