Design, Engineering and Discovery of Novel α-Helical and β-Boomerang Antimicrobial Peptides against Drug Resistant Bacteria

Surajit Bhattacharjya; Suzana K Straus

doi:10.3390/ijms21165773

Design, Engineering and Discovery of Novel α-Helical and β-Boomerang Antimicrobial Peptides against Drug Resistant Bacteria

Int J Mol Sci. 2020 Aug 11;21(16):5773. doi: 10.3390/ijms21165773.

Authors

Surajit Bhattacharjya¹, Suzana K Straus²

Affiliations

¹ School of Biological Sciences, 60 Nanyang Drive, Nanyang Technological University, Singapore 637551, Singapore.
² Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC V6T 1Z1, Canada.

Abstract

In an era where the pipeline of new antibiotic development is drying up, the continuous rise of multi-drug resistant (MDR) and extensively drug resistant (XDR) bacteria are genuine threats to human health. Although antimicrobial peptides (AMPs) may serve as promising leads against drug resistant bacteria, only a few AMPs are in advanced clinical trials. The limitations of AMPs, namely their low in vivo activity, toxicity, and poor bioavailability, need to be addressed. Here, we review engineering of frog derived short α-helical AMPs (aurein, temporins) and lipopolysaccharide (LPS) binding designed β-boomerang AMPs for further development. The discovery of novel cell selective AMPs from the human proprotein convertase furin is also discussed.

Keywords: antimicrobial peptides (AMPs); extensively drug resistant (XDR) bacteria; lipopolysaccharide (LPS) binding; multi-drug resistant (MDR) bacteria; α-helical and β-boomerang AMPs.

Publication types

Review

MeSH terms

Amino Acid Sequence
Biological Availability
Drug Design*
Drug Resistance, Bacterial*
Humans
Pore Forming Cytotoxic Proteins / chemistry*
Pore Forming Cytotoxic Proteins / pharmacology*
Protein Engineering*
Protein Structure, Secondary

Substances

Pore Forming Cytotoxic Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding