High-performance liquid chromatography and mass spectrometry-based design of proteolytically stable antimicrobial peptides

Mojtaba Bagheri, Robert Hancock

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Citations (Scopus)

Abstract

The emergence of multiresistant bacteria worldwide together with the shortage of effective antibiotics in the market emphasizes the need for the design and development of the promising agents for the treatment of superbug-associated infections. Antimicrobial peptides (AMPs) have been considered as excellent candidates to tackle this issue, and thousands of peptides of different lengths, amino acid compositions, and mode of action have been discovered and prepared to date. Nevertheless, it is of great importance to develop innovative formulation strategies for delivering these AMPs and to improve their low bioavailability and metabolic stability, particularly against proteases, if these peptides are to find applications in the clinic and administered orally or parenterally or used as dietary supplements. The purpose of this chapter is to describe basic experimental principles, based on analytical reversed-phase high-performance liquid chromatography (RP-HPLC) and mass spectrometry (MS), for the prospective design of orally bioavailable AMPs considering the structural characteristics of the peptides and the substrate specificity of proteases that abound in the body especially at sites of infection.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages61-71
Number of pages11
DOIs
Publication statusPublished - 1 Jan 2017
Externally publishedYes

Publication series

NameMethods in Molecular Biology
Volume1548
ISSN (Print)1064-3745

Keywords

  • Antimicrobial peptides
  • Bioavailability
  • Mass spectrometry
  • Proteases
  • Reversed-phase high-performance liquid chromatography

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Bagheri, M., & Hancock, R. (2017). High-performance liquid chromatography and mass spectrometry-based design of proteolytically stable antimicrobial peptides. In Methods in Molecular Biology (pp. 61-71). (Methods in Molecular Biology; Vol. 1548). Humana Press Inc.. https://doi.org/10.1007/978-1-4939-6737-7_5