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

Research output: Contribution to journalArticlepeer-review

17 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crystals that contain the d form of the magainin 2 derivative along with an l-peptide in which one Ala has been replaced by a β-amino acid residue.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 languageAmerican English
Pages (from-to)11884-11887
Number of pages4
JournalJournal of the American Chemical Society
Volume137
Issue number37
DOIs
StatePublished - 23 Sep 2015

Bibliographical note

Publisher Copyright:
© 2015 American Chemical Society.

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