Turn-off enzyme activity of histidine-rich peptides for the detection of lysozyme

Zu Han Yang, Ling Fang Huang, Yi Shan Wang, Chia Chen Chang*

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

Abstract

An assay that integrates histidine-rich peptides (HisRPs) with high-affinity aptamers was developed enabling the specific and sensitive determination of the target lysozyme. The enzyme-like activity of HisRP is inhibited by its interaction with a target recognized by an aptamer. In the presence of the target, lysozyme molecules progressively assemble on the surface of HisRP in a concentration-dependent manner, resulting in the gradual suppression of enzyme-like activity. This inhibition of HisRP's enzyme-like activity can be visually observed through color changes in the reaction product or quantified using UV-visible absorption spectroscopy. Under optimal conditions, the proposed colorimetric assay for lysozyme had a detection limit as low as 1 nM and exhibited excellent selectivity against other nonspecific interferents. Furthermore, subsequent research validated the practical applicability of the developed colorimetric approach to saliva samples, indicating that the assay holds significant potential for the detection of lysozymes in samples derived from humans.

Original languageEnglish
Article number307
Pages (from-to)307
JournalMicrochimica Acta
Volume191
Issue number6
DOIs
StatePublished - 07 05 2024

Bibliographical note

© 2024. The Author(s), under exclusive licence to Springer-Verlag GmbH Austria, part of Springer Nature.

Keywords

  • Colorimetric assay
  • Histidine-rich peptide
  • Lysozyme aptamer
  • Lysozyme determination
  • Histidine/analysis
  • Limit of Detection
  • Proteins/analysis
  • Humans
  • Peptides/chemistry
  • Biosensing Techniques/methods
  • Muramidase/analysis
  • Colorimetry/methods
  • Saliva/chemistry
  • Aptamers, Nucleotide/chemistry

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