Hemolytic and Antimicrobial Activities of the Twenty-Four Individual Omission Analogues of Melittin Article

Blondelle, SE, Houghten, RA. (1991). Hemolytic and Antimicrobial Activities of the Twenty-Four Individual Omission Analogues of Melittin . BIOCHEMISTRY, 30(19), 4671-4678. 10.1021/bi00233a006

cited authors

  • Blondelle, SE; Houghten, RA

abstract

  • Although melittin’s hemolytic activity has been extensively studied, the orientation of membrane-bound melittin remains uncertain. We have investigated the effect of individually omitted amino acid residues on melittin’s activity and related these results to the existing models of melittin-membrane interaction. The extent of hemolysis of the omission analogues closely followed the four known conformational regions of melittin: omission of any of the residues making up the two α-helical regions decreased the hemolytic activity relative to melittin, while omission of any of the residues making up the “hinge” or the C-terminal regions had little or no effect. Our results correlate best with a proposed model in which melittin initially forms “holes” in the membrane, resulting in an initial rapid loss of hemoglobin; the membrane-bound melittin is then internalized into the membrane, resulting in a later slow phase of hemoglobin loss. It was also found that induced structural effects caused by peptide-lipid interactions could be studied by using RP-HPLC., with an excellent correlation found between the retention times of the individual omission analogues and their hemolytic activities. © 1991, American Chemical Society. All rights reserved.

publication date

  • May 1, 1991

published in

Digital Object Identifier (DOI)

start page

  • 4671

end page

  • 4678

volume

  • 30

issue

  • 19