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Effect of melittin and melittin fragments on the thermotropic phase transition of dipalmitoyllecithin and on the amount of lipid‐bound water
Author(s) -
Mollay Christa
Publication year - 1976
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(76)80250-5
Subject(s) - melittin , thermotropic crystal , chemistry , phase transition , physics , philosophy , art history , phase (matter) , art , thermodynamics , biochemistry , organic chemistry , peptide , liquid crystalline
Melittin is the main cytolytic component of bee venom [l] . The first twenty amino acids of this peptide are mostly apolar whereas the C-terminal hexapeptide is polar and highly basic. The biological activity of melittin has been studied by biochemical and biophysical methods [2-91. Changes in the physical state of membrane phospholipids have been postulated to cause the biological effects of melittin such as increased susceptibility of lipids towards phospholipases AZ [3,7,8] , and at higher peptide concentrations, complete lysis of cells [2]. Melittin interacts with phospholipids both in liposomes [6] and in biomembranes [6,8] . According to recent evidence, this interaction causes a decrease in the mobility of the fatty acid chains and a rearrangement of the headgroup of phosphatides [S] . The hydrophobic segment of melittin, corresponding to the first nineteen residues (designated mell__rr,) and the basic heptapeptide (melae-s6) can be isolated. The effects of melittin and of these characteristic fragments on the gel to liquid crystalline phasetransition of dipalmitoylphosphatidylcholine and the amount of lipid bound water are described in this paper.