Evidence map›Paper›PMID 22401132›Full record

ArticleJournal of the American Chemical Society2012

Sequence, structure, and function of peptide self-assembled monolayers.

Ann K Nowinski, Fang Sun, Andrew D White, Andrew J Keefe, Shaoyi Jiang

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
10.2field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 308 citations in OpenAlex.

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  19. Modular Design for Proteins Assembling into Antifouling Coatings: Case of Gold Surfaces.Langmuir : the ACS journal of surfaces and colloids · 2023
    Article
  20. 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 1 institution in 1 country.

Ann K NowinskiDepartment of Chemical Engineering, University of Washington, Seattle, Washington 98195, USA.
Fang Sun
Andrew D White
Andrew J Keefe
Shaoyi Jiang
University of Washington · US

Funding

Surface Analysis Facility for Biomedical ProblemsP41EB002027 · NIBIB · UNIVERSITY OF WASHINGTON · PI CASTNER, DAVID G, GAMBLE, LARA · 2003 to 2019
$17.6M
NIBIB NIH HHS EB-002027NIBIB NIH HHS P41 EB002027
6 · The paper itself

Abstract

Cysteine is commonly used to attach peptides onto gold surfaces. Here we show that the inclusion of an additional linker with a length of four residues (-PPPPC) and a rigid, hydrophobic nature is a better choice for forming peptide self-assembled monolayers (SAMs) with a well-ordered structure and high surface density. We compared the structure and function of the nonfouling peptide EKEKEKE-PPPPC-Am with EKEKEKE-C-Am. Circular dichroism, attenuated total internal reflection Fourier transform IR spectroscopy, and molecular dynamics results showed that EKEKEKE-PPPPC-Am forms a secondary structure while EKEKEKE-C-Am has a random structure. Surface plasmon resonance sensor results showed that protein adsorption on EKEKEKE-PPPPC-Am/gold is very low with small variation while protein adsorption on EKEKEKE-C-Am/gold is high with large variation. X-ray photoelectron spectroscopy results showed that both peptides have strong gold-thiol binding with the gold surface, indicating that their difference in protein adsorption is due to their assembled structures. Further experimental and simulation studies were performed to show that -PPPPC is a better linker than -PC, -PPC, and -PPPC. Finally, we extended EKEKEKE-PPPPC-Am with the cell-binding sequence RGD and demonstrated control over specific versus nonspecific cell adhesion without using poly(ethylene glycol). Adding a functional peptide to the nonfouling EK sequence avoids complex chemistries that are used for its connection to synthetic materials.

Indexed as

BiofoulingAmino Acid SequenceGoldModels, MolecularOligopeptidesProtein Structure, SecondarySolutionsSurface PropertiesGoldOligopeptidesSolutions

Identifiers

PMID22401132
PMCPMC3826823
OpenAlexW2050445499

What OpenQuestion holds

Textmetadata
LicenceTDM
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.