Binary Encoding of Random Peptide Sequences for Selective and Differential Antimicrobial Mechanisms

Zvi Hayouka*, Angelo Bella, Tal Stern, Santanu Ray, Haibo Jiang, Chris R.M. Grovenor, Maxim G. Ryadnov

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


Binary encoding of peptide sequences into differential antimicrobial mechanisms is reported. Such sequences are random in composition, but controllable in chain length, are assembled from the same two amino acids, but differ in the stereochemistry of one. Regardless of chirality, the sequences lyse bacteria including the “superbugs” methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococci (VRE). Sequences with the same chirality, so-called homochiral sequences, assemble into antimicrobial pores and form contiguous helices that are biologically promiscuous and hemolytic. By contrast, heterochiral sequences that lack such persistence selectively attack bacterial membranes without oligomerizing into visible pores. These results offer a mechanistic rationale for designing membrane-selective and sequence-independent antimicrobials.

Original languageAmerican English
Pages (from-to)8099-8103
Number of pages5
JournalAngewandte Chemie - International Edition
Issue number28
StatePublished - 3 Jul 2017

Bibliographical note

Publisher Copyright:
© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim


  • MRSA
  • antibiotics
  • diastereomers
  • fluorescence imaging
  • protein design


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