ArticleCommunications biology2022
Matching amino acids membrane preference profile to improve activity of antimicrobial peptides.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Discovery of potent low-toxicity antimicrobial peptides through diffusion modeling.Nature communications · 2026Article
- Short Antimicrobial Peptides Based on Arginine and Tryptophan: Agents with Potential in Combating Resistant Pathogens.ACS omega · 2026Article
- Precise Construction of an Antimicrobial Peptide Targeting Bacterial Cell Membranes Derived From Natural Peptides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Elucidating the Impact of Red Blood Cell Membrane Components on Melittin-Induced Pore Formation with Molecular Dynamics Simulations.The journal of physical chemistry. B · 2025Article
- Applications of Isothermal Titration Calorimetry in Studying Biomimetic Nanocarriers.Biomolecules · 2025Review
- Insights into the Adsorption Mechanisms of the Antimicrobial Peptide CIDEM-501 on Membrane Models.Antibiotics (Basel, Switzerland) · 2024Article
- Possible Molecular Mechanisms Underlying the Decrease in the Antibacterial Activity of Protamine-like Proteins after Exposure ofInternational journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antimicrobial peptides (AMPs) are cationic antibiotics that can kill multidrug-resistant bacteria via membrane insertion. However, their weak activity limits their clinical use. Ironically, the cationic charge of AMPs is essential for membrane binding, but it obstructs membrane insertion. In this study, we postulate that this problem can be overcome by locating cationic amino acids at the energetically preferred membrane surface. All amino acids have an energetically preferred or less preferred membrane position profile, and this profile is strongly related to membrane insertion. However, most AMPs do not follow this profile. One exception is protegrin-1, a powerful but neglected AMP. In the present study, we found that a potent AMP, WCopW5, strongly resembles protegrin-1 and that the match between its sequence and the preferred position profile closely correlates with its antimicrobial activity. One of its derivatives, WCopW43, has antimicrobial activity comparable to that of the most effective AMPs in clinical use.
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Registered trials
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.