Design of single-stranded nucleic acid binding peptides based on nucleocapsid CCHC-box zinc-binding domains

Anthony L. Guerrerio, Jeremy M. Berg

Research output: Contribution to journalArticlepeer-review

Abstract

The solution structures of nucleocapsid (NC)-like CCHC zinc-binding domains bound to nucleic acid targets have revealed that these domains bind guanosine residues within single-stranded nucleic acids. Here, we have performed initial studies examining the potential use of NC-like CCHC zinc-binding domains as modules to construct single-stranded nucleic acid binding peptides. The affinity for guanosine-containing single-stranded deoxyribooligonucleotides increases with the number of CCHC domains in the peptide. The length of the linker between domains affects the spacing of guanosine residues in oligonucleotides that are preferentially bound. These studies provide a proof of principle that NC-like CCHC zinc-binding domains can be utilized as a basis for designing peptides that bind specific single-stranded nucleic acid sequences.

Original languageEnglish (US)
Pages (from-to)9638-9643
Number of pages6
JournalJournal of the American Chemical Society
Volume132
Issue number28
DOIs
StatePublished - Jul 21 2010

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Fingerprint Dive into the research topics of 'Design of single-stranded nucleic acid binding peptides based on nucleocapsid CCHC-box zinc-binding domains'. Together they form a unique fingerprint.

Cite this