ArticlePeerJ2015
Differential scanning calorimetry of whole Escherichia coli treated with the antimicrobial peptide MSI-78 indicate a multi-hit mechanism with ribosomes as a novel target.
Article in PeerJ, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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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.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Biomolecules involved in the metabolism of Escherichia coli affected by photodynamics: A calorimetry study.PloS one · 2026Article
- Cytoplasmic fluidity and the cold life: proteome stability is decoupled from viability in psychrophiles.Nature communications · 2025Article
- Assessment of Arthrobacter oxydans Subcellular Structural Stability in Response to Metal Action using Differential Scanning Calorimetry.Cell biochemistry and biophysics · 2025Article
- Terahertz thermal curve analysis for label-free identification of pathogens.Nature communications · 2022Article
- Antimicrobial Peptide Mechanisms Studied by Whole-Cell Deuterium NMR.International journal of molecular sciences · 2022Review
- Fever temperatures impair hemolysis caused by strains ofHeliyon · 2022Article
- Role of lipopolysaccharide in antimicrobial and cell penetrating peptide membrane interactions probed by deuterium NMR of whole cells.BBA advances · 2022Article
- Deuterium Solid State NMR Studies of Intact Bacteria Treated With Antimicrobial Peptides.Frontiers in medical technology · 2020Review
- Mechanisms of Action for Antimicrobial Peptides With Antibacterial and Antibiofilm Functions.Frontiers in microbiology · 2019Review
- Article
- Mechanistic and structural basis of bioengineered bovine Cathelicidin-5 with optimized therapeutic activity.Scientific reports · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Differential Scanning Calorimetry (DSC) of intact Escherichia coli (E. coli) was used to identify non-lipidic targets of the antimicrobial peptide (AMP) MSI-78. The DSC thermograms revealed that, in addition to its known lytic properties, MSI-78 also has a striking effect on ribosomes. MSI-78's effect on DSC scans of bacteria was similar to that of kanamycin, an antibiotic drug known to target the 30S small ribosomal subunit. An in vitro transcription/translation assay helped confirm MSI-78's targeting of ribosomes. The scrambled version of MSI-78 also affected the ribosome peak of the DSC scans, but required greater amounts of peptide to cause a similar effect to the unscrambled peptide. Furthermore, the effect of the scrambled peptide was not specific to the ribosomes; other regions of the DSC thermogram were also affected. These results suggest that MSI-78's effects on E. coli are at least somewhat dependent on its particular structural features, rather than a sole function of its overall charge and hydrophobicity. When considered along with earlier work detailing MSI-78's membrane lytic properties, it appears that MSI-78 operates via a multi-hit mechanism with multiple targets.
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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.