Abstract:
:In spite of numerous studies, there appears to be no consensus regarding the orientation and aggregation state of membrane-bound melittin. We report here the restricted environment of the sole tryptophan residue in membrane-bound melittin using environment-induced effects on the rates of solvent relaxation. When incorporated into unilamellar vesicles of dioleoyl-sn-glycero-3-phosphocholine (DOPC), melittin exhibits a red edge excitation shift (REES) of 5 nm. In addition, fluorescence polarization of melittin in the membrane shows both excitation and emission wavelength dependence. Taken together, these observations indicate that the tryptophan residue of melittin is located in a motionally restricted region in the membrane.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Chattopadhyay A,Rukmini Rdoi
10.1016/0014-5793(93)80415-qsubject
Has Abstractpub_date
1993-12-13 00:00:00pages
341-4issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(93)80415-Qjournal_volume
335pub_type
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