ArticlePeptides2008
Correlation between simulated physicochemical properties and hemolycity of protegrin-like antimicrobial peptides: predicting experimental toxicity.
Article in Peptides, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 48 citations in OpenAlex.
- Article
- Peptide hemolytic activity analysis using visual data mining of similarity-based complex networks.NPJ systems biology and applications · 2024Article
- Design of Protegrin-1 Analogs with Improved Antibacterial Selectivity.Pharmaceutics · 2023Article
- Combined Use of Antimicrobial Peptides with Antiseptics against Multidrug-Resistant Bacteria: Pros and Cons.Pharmaceutics · 2023Article
- Traditional and Computational Screening of Non-Toxic Peptides and Approaches to Improving Selectivity.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy.European biophysics journal : EBJ · 2017Article
- Distinct profiling of antimicrobial peptide families.Bioinformatics (Oxford, England) · 2015Article
- Expression of porcine protegrin-1 inExperimental and therapeutic medicine · 2015Article
- AtomicChargeCalculator: interactive web-based calculation of atomic charges in large biomolecular complexes and drug-like molecules.Journal of cheminformatics · 2015Article
- Multiscale Models of Antibiotic Probiotics.Current opinion in chemical engineering · 2014Article
- Article
- Multiscale models of the antimicrobial peptide protegrin-1 on gram-negative bacteria membranes.International journal of molecular sciences · 2012Review
- Knowledge-based computational methods for identifying or designing novel, non-homologous antimicrobial peptides.European biophysics journal : EBJ · 2011Article
- Review
- Exploring the pharmacological potential of promiscuous host-defense peptides: from natural screenings to biotechnological applications.Frontiers in microbiology · 2011Article
- Antimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studies.Biophysical journal · 2010Article
- Free energy profile of the interaction between a monomer or a dimer of protegrin-1 in a specific binding orientation and a model lipid bilayer.The journal of physical chemistry. B · 2010Article
- Antimicrobial mechanism of pore-forming protegrin peptides: 100 pores to kill E. coli.Peptides · 2010Article
- Relative free energy of binding between antimicrobial peptides and SDS or DPC micelles.Molecular simulation · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The therapeutic, antibiotic potential of antimicrobial peptides can be prohibitively diminished because of the cytotoxicity and hemolytic profiles they exhibit. Quantifying and predicting antimicrobial peptide toxicity against host cells is thus an important goal of AMP related research. In this work, we present quantitative structure activity relationships for toxicity of protegrin-like antimicrobial peptides against human cells (epithelial and red blood cells) based on physicochemical properties, such as interaction energies and radius of gyration, calculated from molecular dynamics simulations of the peptides in aqueous solvent. The hypothesis is that physicochemical properties of peptides, as manifest by their structure and interactions in a solvent and as captured by atomistic simulations, are responsible for their toxicity against human cells. Protegrins are beta-hairpin peptides with high activity against a wide variety of microbial species, but in their native state are toxic to human cells. Sixty peptides with experimentally determined toxicities were used to develop the models. We test the resulting relationships to determine their ability to predict the toxicity of several protegrin-like peptides. The developed QSARs provide insight into the mechanism of cytotoxic action of antimicrobial peptides. In a subsequent blind test, the QSAR correctly ranked four of five protegrin analogues newly synthesized and tested for toxicity.
Indexed as
Identifiers
What OpenQuestion holds
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.