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Structure and activity studies of pardaxin and analogues using model membranes of phosphatidylcholine

journal contribution
posted on 1992-12-09, 00:00 authored by Colin BarrowColin Barrow, Koji Nakanishi, Kazuo Tachibana
Thirteen synthetic pardaxin analogues were assayed for their ability to interact with model membranes of phosphatidylcholine. The results suggested the following: An amphipathic α-helix from isoleucine-14 to leucine-26 is responsible for most of the membrane perturbing properties of pardaxin. A hydrophobic N-terminal region enhances the activity of the isoleucine-14 to leucine-26 α-helix by binding the pardaxin molecule to the lipid bilayer. A bend centered around 12Ser-13Pro appears to create overall amphipathicity for the two different helical regions of pardaxin, but this contributes only slightly to potency. The C-terminal amino acids are unimportant for membrane perturbing activity and may be present only to enhance transportation in an aqueous environment prior to membrane binding in the native system. © 1992.

History

Journal

BBA - Biomembranes

Volume

1112

Issue

2

Pagination

235 - 240

ISSN

0005-2736

Publication classification

CN.1 Other journal article