Evidence for phenylalanine zipper-mediated dimerization in the X-ray crystal structure of a magainin 2 analogue

Zvi Hayouka, David E. Mortenson, Dale F. Kreitler, Bernard Weisblum, Katrina T. Forest, Samuel H. Gellman*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

High-resolution structure elucidation has been challenging for the large group of host-defense peptides that form helices on or within membranes but do not manifest a strong folding propensity in aqueous solution. Here we report the crystal structure of an analogue of the widely studied host-defense peptide magainin 2. Magainin 2 (S8A, G13A, G18A) is a designed variant that displays enhanced antibacterial activity relative to the natural peptide. The crystal structure of magainin 2 (S8A, G13A, G18A), obtained for the racemic form, features a dimerization mode that has previously been proposed to play a role in the antibacterial activity of magainin 2 and related peptides.

Original languageAmerican English
Pages (from-to)15738-15741
Number of pages4
JournalJournal of the American Chemical Society
Volume135
Issue number42
DOIs
StatePublished - 23 Oct 2013
Externally publishedYes

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