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:https://doi.org/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

Institute of Biochemistry, Food Science and Nutrition

The Hebrew University of Jerusalem

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

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crystals that contain the d form of the magainin 2 derivative along with an l-peptide in which one Ala has been replaced by a β-amino acid residue.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

All Science Journal Classification (ASJC) codes

General Chemistry
Biochemistry
Catalysis
Colloid and Surface Chemistry

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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.",

author = "Zvi Hayouka and Thomas, {Nicole C.} and Mortenson, {David E.} and Satyshur, {Kenneth A.} and Bernard Weisblum and Forest, {Katrina T.} and Gellman, {Samuel H.}",

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doi = "https://doi.org/10.1021/jacs.5b07206",

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T1 - Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif

AU - Hayouka, Zvi

AU - Thomas, Nicole C.

AU - Mortenson, David E.

AU - Satyshur, Kenneth A.

AU - Weisblum, Bernard

AU - Forest, Katrina T.

AU - Gellman, Samuel H.

PY - 2015/9/23

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N2 - 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.

AB - 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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U2 - https://doi.org/10.1021/jacs.5b07206

DO - https://doi.org/10.1021/jacs.5b07206

M3 - مقالة

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SN - 0002-7863

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SP - 11884

EP - 11887

JO - Journal of the American Chemical Society

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IS - 37

ER -

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

Abstract

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