The effect of counterions on melittin aggregation
- 1 June 1983
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 211 (3) , 683-686
- https://doi.org/10.1042/bj2110683
Abstract
Melittin, a surface-active polypeptide from bee venom, has an overall hydrophobic N-terminus, with basic residues clustered at the C-terminus. In aqueous solution melittin exists as a mixture of monomer and tetramer, the monomer adopting a predominantly random-coil configuration, whereas the tetramer is rich in α-helix. The tendency of melittin to aggregate is dependent on the counter-anions present in solution, the effect being most marked with phosphate, decreasing in the order HPO4(2-) greater than SO4(2-) greater than ClO4- greater than Cl-.This publication has 30 references indexed in Scilit:
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