The effect of counterions on melittin aggregation

A. S. Tatham; R. C. Hider; A. F. Drake

doi:10.1042/bj2110683

The effect of counterions on melittin aggregation

A. S. Tatham^*, R. C. Hider, A. F. Drake

^*Corresponding author for this work

Cardiff School of Sport and Health Sciences

Research output: Contribution to journal › Article › peer-review

31 Citations (Scopus)

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 alpha-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-.

Original language	English
Pages (from-to)	683-686
Number of pages	4
Journal	The Biochemical journal
Volume	211
Issue number	3
DOIs	https://doi.org/10.1042/bj2110683
Publication status	Published - 1 Jun 1983

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AU - Drake, A. F.

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N2 - 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 alpha-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-.

AB - 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 alpha-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-.

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JF - The Biochemical journal

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The effect of counterions on melittin aggregation

Abstract

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