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

doi:10.1021/ja409082w

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 journal › Article › peer-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 language	English
Pages (from-to)	15738-15741
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	135
Issue number	42
DOIs	https://doi.org/10.1021/ja409082w
State	Published - 23 Oct 2013
Externally published	Yes

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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.",

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AU - Weisblum, Bernard

AU - Forest, Katrina T.

AU - Gellman, Samuel H.

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AB - 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.

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

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