Evidence map›Paper›PMID 9251822›Full record

ArticleBiophysical journal1997

Formation of stable polypeptide monolayers at interfaces: controlling molecular conformation and orientation.

M Boncheva, H Vogel

Abstract read
In one paragraph

Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Multifaceted aspects of charge transfer.Physical chemistry chemical physics : PCCP · 2020
    Article
  5. Article
  6. Article
  7. On-surface assembly of coiled-coil heterodimers.Langmuir : the ACS journal of surfaces and colloids · 2012
    Article
  8. Sequence, structure, and function of peptide self-assembled monolayers.Journal of the American Chemical Society · 2012
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Stable self-assembly of a protein engineering scaffold on gold surfaces.Protein science : a publication of the Protein Society · 2002
    Article
  15. Self-assembly of the hydrophobin SC3 proceeds via two structural intermediates.Protein science : a publication of the Protein Society · 2002
    Article
  16. Peptide interfacial adsorption is kinetically limited by the thermodynamic stability of self association.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  17. Article
  18. 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

2 authors.

M BonchevaInstitute of Physical Chemistry, Swiss Federal Institute of Technology, Lausanne, Switzerland.
H Vogel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The molecular self-organization and structural properties of peptide assemblies at different interfaces, using either amphipathic or hydrophobic polypeptide helices, is described. The two peptides under investigation form stable monolayers on the water surface under the conservation of their molecular conformation, as studied by circular dichroism and polarization-modulation Fourier transform infrared (FTIR) spectroscopy. Using surface plasmon resonance and reflection-absorption FTIR, we show that such molecular layers can be transferred unaltered to solid substrates. Most importantly, the molecular orientation of the hydrophobic helices on solid supports such as gold can be controlled by choosing a particular procedure for the layer formation. The helices were oriented parallel to the interface in Langmuir-Blodgett monolayers, and perpendicular to the interface in self-assembled monolayers. Our reflection-absorption FTIR measurements have delivered for the first time direct experimental evidence for the molecular conformation and orientation of pure peptide monolayers. Suitable reference spectra of polypeptides with defined conformation and orientation are necessary to use this technique for the determination of the molecular orientation of peptides in monomolecular films. We have solved the problem for alpha-helical polypeptides by using bacteriorhodopsin as a reference in combination with synthetic alpha-helices of defined interfacial orientation. The present study shows the possibility of constructing immobilized peptide monolayers with predefined macroscopic properties and molecular structure by choosing the proper polypeptide amino acid sequence, the technique used for layer formation, and the supporting surface properties.

Indexed as

Protein ConformationProtein FoldingProtein Structure, SecondaryAmino Acid SequenceBinding SitesModels, ChemicalModels, MolecularModels, StructuralMolecular Sequence DataPeptidesSpectroscopy, Fourier Transform InfraredPeptides

Identifiers

PMID9251822
PMCPMC1181002

What OpenQuestion holds

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Registered trials

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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.