Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif

Zvi Hayouka; Nicole C. Thomas; David E. Mortenson; Kenneth A. Satyshur; Bernard Weisblum; Katrina T. Forest; Samuel H. Gellman

doi:10.1021/jacs.5b07206

Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif

Zvi Hayouka, Nicole C. Thomas, David E. Mortenson, Kenneth A. Satyshur, Bernard Weisblum, Katrina T. Forest^*, Samuel H. Gellman

^*Corresponding author for this work

Institute of Biochemistry, Food Science and Nutrition

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

18 Scopus citations

Abstract

Quasiracemic crystallography has been used to explore the significance of homochiral and heterochiral associations in a set of host-defense peptide derivatives. The previously reported racemic crystal structure of a magainin 2 derivative displayed a homochiral antiparallel dimer association featuring a "phenylalanine zipper" notable for the dual roles of phenylalanines in mediating dimerization and formation of an exposed hydrophobic swath. This motif is seen as well in two new quasiracemate crystals that contain the d form of the magainin 2 derivative along with an l-peptide in which one Ala has been replaced by a β-amino acid residue. This structural trend supports the hypothesis that the Phe zipper motif has functional significance.

Original language	English
Pages (from-to)	11884-11887
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	137
Issue number	37
DOIs	https://doi.org/10.1021/jacs.5b07206
State	Published - 23 Sep 2015

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© 2015 American Chemical Society.

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title = "Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif",

abstract = "Quasiracemic crystallography has been used to explore the significance of homochiral and heterochiral associations in a set of host-defense peptide derivatives. The previously reported racemic crystal structure of a magainin 2 derivative displayed a homochiral antiparallel dimer association featuring a {"}phenylalanine zipper{"} notable for the dual roles of phenylalanines in mediating dimerization and formation of an exposed hydrophobic swath. This motif is seen as well in two new quasiracemate crystals that contain the d form of the magainin 2 derivative along with an l-peptide in which one Ala has been replaced by a β-amino acid residue. This structural trend supports the hypothesis that the Phe zipper motif has functional significance.",

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AU - Mortenson, David E.

AU - Satyshur, Kenneth A.

AU - Weisblum, Bernard

AU - Forest, Katrina T.

AU - Gellman, Samuel H.

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Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif

Abstract

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