The pH sensitivity of histidine-containing lytic peptides

Zhigang Tu, Albert Young, Christopher Murphy, Jun F. Liang

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

Abstract

Many bioactive peptides are featured by their unique amino acid compositions such as argine/lysine-rich peptides. However, histidine-rich bioactive peptides are hardly found. In this study, histidine-containing peptides were constructed by selectively replacing the corresponded lysine residues in a lytic peptide LL-1 with histidines. Interestingly, all resulting peptides demonstrated pH-dependent activities. The cell lysis activities of these peptides could be increased up to four times as the solution pHs dropped from pH = 7.4 to pH = 5.5. The pH sensitivity of a histidine-containing peptide was determined by histidine substitution numbers. Peptide derivatives with more histidines were associated with increased pH sensitivity. Results showed that not the secondary structures but pH-affected cell affinity changes were responsible for the pH-dependent activities of histidine-containing peptides. The histidine substitution approach demonstrated here may present a general strategy to construct bioactive peptides with desired pH sensitivity for various applications.

Original languageEnglish
Pages (from-to)790-795
Number of pages6
JournalJournal of Peptide Science
Volume15
Issue number11
DOIs
StatePublished - Nov 2009

Keywords

  • Bioactive
  • Cell lysis
  • Histidine
  • Peptide
  • pH sensitivity

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