ArticleJournal of the American Chemical Society2009
Metal-binding dependent disruption of membranes by designed helices.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 32 citations in OpenAlex.
- A Glimpse in the Metal Ion Selectivity Rules: Zn(II), Cd(II) and Co(II) Interplay With Different Protein Coordination Spheres in Determining Variable Thermal Stability and Folding Scenarios.Bioinorganic chemistry and applications · 2026Article
- Review
- Article
- Micelle-Triggered β-Hairpin to α-Helix Transition in a 14-Residue Peptide from a Choline-Binding Repeat of the Pneumococcal Autolysin LytA.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- Functional, metal-based crosslinkers for α-helix induction in short peptides.Chemical science · 2013Article
- Antimicrobial action of the cyclic peptide bactenecin on Burkholderia pseudomallei correlates with efficient membrane permeabilization.PLoS neglected tropical diseases · 2013Article
- Computational studies of membrane proteins: models and predictions for biological understanding.Biochimica et biophysica acta · 2012Review
- Computational design of membrane proteins.Structure (London, England : 1993) · 2012Review
- Computational protein design: engineering molecular diversity, nonnatural enzymes, nonbiological cofactor complexes, and membrane proteins.Current opinion in chemical biology · 2011Review
- Copper(II) enhances membrane-bound α-synuclein helix formation.Metallomics : integrated biometal science · 2011Article
- Proteins that switch folds.Current opinion in structural biology · 2010Review
- Computational protein design: Advances in the design and redesign of biomolecular nanostructures.Current opinion in colloid & interface science · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The de novo design of molecular switching peptides is of increasing interest because it tests and extends our fundamental understanding of this process while laying the groundwork for the creation of new chemical and biological sensors. Here, an alpha-helical amphiphilic cell-lytic peptide, mastoparan X, was engineered to bind divalent cations. Binding of Zn(II) or Ni(II) to the designed peptide Mst-HH stabilizes the lytic amphiphilic structure and increases the activity of the peptide. Although both Zn(II) and Ni(II) activate Mst-HH for membrane lysis, they appear to do so via different mechanisms. Additionally, a series of metal binding-site mutants were synthesized to assess the relationship of charge and helical propensity to the toxicity and switchability. Additionally, by changing the characteristics of the metal-binding ligands, we can vary the selectivity of the site.
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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.