Evidence map›Paper›PMID 16935948›Full record

ArticleBiophysical journal2006

Phenol red interacts with the protofibril-like oligomers of an amyloidogenic hexapeptide NFGAIL through both hydrophobic and aromatic contacts.

Chun Wu, Hongxing Lei, Zhixiang Wang, Wei Zhang, Yong Duan

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2006. 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
1.0field-weighted citation impact, top 24% 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

18 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. The Impact of Halogenated Phenylalanine Derivatives on NFGAIL Amyloid Formation.Chembiochem : a European journal of chemical biology · 2020
    Article
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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.

Chun WuGenome Center and Department of Applied Science, University of California, Davis, California 95616, USA.
Hongxing Lei
Zhixiang Wang
Wei Zhang
Yong Duan
University of California, Davis · US

Funding

Toward experimental quality protein structures: a synergistic approachR01GM067168 · NIGMS · UNIVERSITY OF DELAWARE · PI DUAN, YONG, ZHOU, YAOQI · 2003 to 2012
$2.4M
Formation mechanisms of native states of small proteinsR01GM064458 · NIGMS · UNIVERSITY OF DELAWARE · PI DUAN, YONG · 2002 to 2006
$1.1M
NIGMS NIH HHS GM64458NIGMS NIH HHS GM67168NIGMS NIH HHS R01 GM064458NIGMS NIH HHS R01 GM067168
6 · The paper itself

Abstract

Amyloid-associated diseases affect millions of people worldwide. Phenol red exhibits modest inhibition toward fibril formation of human Islet amyloid polypeptide (hIAPP) and its toxicity, which is associated with type II diabetes mellitus. However, the molecular level mechanisms of interactions remain elusive. The binding of phenol red molecules to the protofibrils of an amyloidogenic fragment (NFGAIL) of hIAPP has been investigated by molecular dynamics simulations with explicit solvent. The phenol red molecules were observed to bind primarily along either beta-sheet stacking or beta-strand directions. Through its three aromatic rings, the phenol red molecule preferentially interacted with the hydrophobic side chains of Phe, Leu, and Ile; and the polar sulfone and hydroxyl groups were mainly exposed in solvent. Thus, phenol red improves the solubility of the early protofibrils and represses further growth. Interestingly, there was no obvious preference toward the aromatic Phe residue in comparison to the hydrophobic Leu or Ile residues. The lack of binding along the hydrogen bond direction indicates that phenol red does not directly block the beta-sheet extension. Further free energy analysis suggested that a phenol red analog may potentially improve the binding affinity.

Indexed as

Models, ChemicalModels, MolecularAmyloidBinding SitesComputer SimulationDimerizationHydrocarbons, AromaticHydrophobic and Hydrophilic InteractionsPeptidesPhenolsulfonphthaleinProtein BindingProtein ConformationAmyloidHydrocarbons, AromaticPeptidesPhenolsulfonphthalein

Identifiers

PMID16935948
PMCPMC1630471
OpenAlexW2130015508

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.