Journal
FRONTIERS IN CHEMISTRY
Volume 8, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fchem.2020.607769
Keywords
70S ribosome; AMPs; antimicrobial peptides; DnaK; host defense peptides; PrAMP; proline-rich antimicrobial peptide
Categories
Funding
- NHMRC [APP1142472, APP1158841, APP1185426]
- ARC [DP160101312, LE200100163]
- Cancer Council Victoria [APP1163284]
- Australian Dental Research
- Centre for Oral Health Research at The Melbourne Dental School
- Weary Dunlop Foundation
- University of Melbourne
- Victorian Government Operational Infrastructure Support Program
- Australian Research Council [LE200100163] Funding Source: Australian Research Council
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As we rapidly approach a post-antibiotic era in which multi-drug resistant bacteria are ever-pervasive, antimicrobial peptides (AMPs) represent a promising class of compounds to help address this global issue. AMPs are best-known for their membrane-disruptive mode of action leading to bacteria cell lysis and death. However, many AMPs are also known to be non-lytic and have intracellular modes of action. Proline-rich AMPs (PrAMPs) are one such class, that are generally membrane permeable and inhibit protein synthesis leading to a bactericidal outcome. PrAMPs are highly effective against Gram-negative bacteria and yet show very low toxicity against eukaryotic cells. Here, we review both the PrAMP family and the past and current definitions for this class of peptides. Computational analysis of known AMPs within the DRAMP database () and assessment of their PrAMP-like properties have led us to develop a revised definition of the PrAMP class. As a result, we subsequently identified a number of unknown and unclassified peptides containing motifs of striking similarity to known PrAMP-based DnaK inhibitors and propose a series of new sequences for experimental evaluation and subsequent addition to the PrAMP family.
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