ArticleJournal of the American Chemical Society2015
Quasiracemate Crystal Structures of Magainin 2 Derivatives Support the Functional Significance of the Phenylalanine Zipper Motif.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Structure of a barrel-stave pore formed by magainin-2 reveals anion selectivity and zipper-mediated assembly.Scientific reports · 2025Article
- Antimicrobial peptides: from discovery to developmental applications.Applied and environmental microbiology · 2025Review
- Roles of inter- and intramolecular tryptophan interactions in membrane-active proteins revealed by racemic protein crystallography.Communications chemistry · 2023Article
- D-Peptide and D-Protein Technology: Recent Advances, Challenges, and Opportunities.Chembiochem : a European journal of chemical biology · 2023Review
- Constructing ion channels from water-soluble α-helical barrels.Nature chemistry · 2021Article
- The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Retention of Native Quaternary Structure in Racemic Melittin Crystals.Journal of the American Chemical Society · 2019Article
- New antimicrobial peptide kills drug-resistant pathogens without detectable resistance.Oncotarget · 2018Article
- The cytotoxicScience (New York, N.Y.) · 2017Article
- X-ray Crystallographic Structure of Oligomers Formed by a Toxic β-Hairpin Derived from α-Synuclein: Trimers and Higher-Order Oligomers.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.