Evidence map›Paper›PMID 18179217›Full record

ArticleJournal of the American Chemical Society2008

Using ion channel-forming peptides to quantify protein-ligand interactions.

Michael Mayer, Vincent Semetey, Irina Gitlin, Jerry Yang, George M Whitesides

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.3field-weighted citation impact, top 8% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Building membrane nanopores.Nature nanotechnology · 2017
    Review
  5. Article
  6. Article
  7. Watching single proteins using engineered nanopores.Protein and peptide letters · 2014
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Gramicidin pores report the activity of membrane-active enzymes.Journal of the American Chemical Society · 2009
    Article
  13. Article
  14. Review
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Michael MayerDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA. mimayer@umich.edu
Vincent Semetey
Irina Gitlin
Jerry Yang
George M Whitesides
University of Michigan–Ann Arbor · USHarvard University · US

Funding

Capillary Electrophoresis and Protein BiophysicsR01GM051559 · NIGMS · HARVARD UNIVERSITY · PI WHITESIDES, GEORGE M · 1994 to 2010
$2.6M
Tools To Study Cell Motility and Ion ChannelsR01GM065364 · NIGMS · HARVARD UNIVERSITY · PI WHITESIDES, GEORGE M · 2003 to 2006
$1.3M
NIGMS NIH HHS GM051559NIGMS NIH HHS GM065364NIGMS NIH HHS R01 GM051559NIGMS NIH HHS R01 GM065364
6 · The paper itself

Abstract

This paper proposes a method for sensing affinity interactions by triggering disruption of self-assembly of ion channel-forming peptides in planar lipid bilayers. It shows that the binding of a derivative of alamethicin carrying a covalently attached sulfonamide ligand to carbonic anhydrase II (CA II) resulted in the inhibition of ion channel conductance through the bilayer. We propose that the binding of the bulky CA II protein (MW approximately 30 kD) to the ion channel-forming peptides (MW approximately 2.5 kD) either reduced the tendency of these peptides to self-assemble into a pore or extracted them from the bilayer altogether. In both outcomes, the interactions between the protein and the ligand lead to a disruption of self-assembled pores. Addition of a competitive inhibitor, 4-carboxybenzenesulfonamide, to the solution released CA II from the alamethicin-sulfonamide conjugate and restored the current flow across the bilayer by allowing reassembly of the ion channels in the bilayer. Time-averaged recordings of the current over discrete time intervals made it possible to quantify this monovalent ligand binding interaction. This method gave a dissociation constant of approximately 2 microM for the binding of CA II to alamethicin-sulfonamide in the bilayer recording chamber: this value is consistent with a value obtained independently with CA II and a related sulfonamide derivative by isothermal titration calorimetry.

Indexed as

IonsAlamethicinBiochemistryCalorimetryInhibitory Concentration 50Ion ChannelsKineticsLigandsLipid BilayersModels, StatisticalMolecular WeightPeptidesProteinsSulfonamidesTime FactorsAlamethicinIon ChannelsIonsLigandsLipid BilayersPeptidesProteinsSulfonamides

Identifiers

PMID18179217
PMCPMC2692494
OpenAlexW1976157304

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.