ArticleFrontiers in chemistry2020
(Re)Defining the Proline-Rich Antimicrobial Peptide Family and the Identification of Putative New Members.
Article in Frontiers in chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 53 citations in OpenAlex.
- Membrane-Traversing Peptides: Mechanistic Landscapes, Assays, and Applications.Chemical reviews · 2026Review
- RmTIL, a cysteine-rich protein as a putative microbiota modulator from Rhipicephalus microplus tick.Parasitology research · 2026Article
- Flipping antimicrobial peptides in the exit tunnel of the bacterial ribosome.Nature communications · 2026Article
- A Localization-Based Motif Combination Approach To the Design of Antimicrobial Peptides Targeting Gram-Positive and Gram-Negative Bacteria.Probiotics and antimicrobial proteins · 2026Article
- Characterization of Proline-Rich Antimicrobial Peptides with SbmA Transporter-Dependent and Independent Antimicrobial Activity towardACS infectious diseases · 2026Article
- Two Shorter Variants of the Proline-Rich Antimicrobial Peptide B7-005 Scaffold Active Against Clinical Isolates ofAntibiotics (Basel, Switzerland) · 2026Article
- A Scoping Review of Snail Antibacterial Peptides and Proteins: From Natural Defence to Translational Prospects.Probiotics and antimicrobial proteins · 2026Article
- Interactions ofInternational journal of molecular sciences · 2025Article
- Designing New Chimeric Proline-Rich Antimicrobial Peptides to Enhance Efficacy Toward the ESKAPE+E: Beyond Sequence Extension.Biomolecules · 2025Article
- The importance role of central proline to the antimicrobial potency and selectivity of indolicidin.Archives of microbiology · 2025Article
- Mixotrophy in Marine Microalgae to Enhance Their Bioactivity.Microorganisms · 2025Article
- Testing antimicrobial peptides inhibiting protein synthesis in livingFrontiers in microbiology · 2025Article
- Proline-Rich Antimicrobial Peptides from Invertebrates.Molecules (Basel, Switzerland) · 2024Review
- Antimicrobial peptides and proteins against drug-resistant pathogens.Cell surface (Amsterdam, Netherlands) · 2024Review
- Stereorandomized Oncocins with Preserved Ribosome Binding and Antibacterial Activity.Journal of medicinal chemistry · 2024Article
- Proline, a unique amino acid whose polymer, polyproline II helix, and its analogues are involved in many biological processes: a review.Amino acids · 2024Review
- Sequence-function mapping of proline-rich antimicrobial peptides.bioRxiv : the preprint server for biology · 2024Article
- Sequence-activity mapping via depletion reveals striking mutational tolerance and elucidates functional motifs in Tur1a antimicrobial peptide.Protein engineering, design & selection : PEDS · 2024Article
- Peptide-based molecules for the disruption of bacterial Hsp70 chaperones.Current opinion in chemical biology · 2023Review
- Antimicrobial Peptides (AMP) in the Cell-Free Culture Media ofAntibiotics (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 (http://dramp.cpu-bioinfor.org/) 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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.