Evidence map›Paper›PMID 29052959›Full record

ArticleChemical biology & drug design2018

Peptide ligands for targeting the extracellular domain of EGFR: Comparison between linear and cyclic peptides.

Tyrslai M Williams, Rushikesh Sable, Sitanshu Singh, Maria Graca H Vicente, Seetharama D Jois

Abstract read
In one paragraph

Article in Chemical biology & drug design, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Analysis of EGFR binding hotspots for design of new EGFR inhibitory biologics.Protein science : a publication of the Protein Society · 2024
    Review
  6. Review
  7. Article
  8. Towards Radiolabeled EGFR-Specific Peptides: Alternatives to GE11.Pharmaceuticals (Basel, Switzerland) · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. 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.

Tyrslai M WilliamsDepartment of Chemistry, Louisiana State University, Baton Rouge, LA, USA.
Rushikesh SableBasic Pharmaceutical Sciences, School of Pharmacy, University of Louisiana at Monroe, Monroe, LA, USA.
Sitanshu SinghBasic Pharmaceutical Sciences, School of Pharmacy, University of Louisiana at Monroe, Monroe, LA, USA.
Maria Graca H VicenteDepartment of Chemistry, Louisiana State University, Baton Rouge, LA, USA.ORCID 0000-0002-4429-7868
Seetharama D JoisBasic Pharmaceutical Sciences, School of Pharmacy, University of Louisiana at Monroe, Monroe, LA, USA.ORCID 0000-0002-6936-772X
University of Louisiana at Monroe · USLouisiana State University · US

Funding

MBRS IMSD Program at Louisiana State UniversityR25GM069743 · NIGMS · LOUISIANA STATE UNIV A&M COL BATON ROUGE · PI VICENTE, MARIA DA GRACA HENRIQUES · 2004 to 2017
$3.4M
CRC-specific near-IR agents for tumor imagingR01CA179902 · NCI · LOUISIANA STATE UNIV A&M COL BATON ROUGE · PI VICENTE, MARIA DA GRACA HENRIQUES · 2014 to 2017
$1.2M
NCI NIH HHS R01 CA179902NIGMS NIH HHS R25 GM069743
6 · The paper itself

Abstract

Colorectal cancer (CRC) is the third most common solid internal malignancy among cancers. Early detection of cancer is key to increasing the survival rate of colorectal cancer patients. Overexpression of the EGFR protein is associated with CRC. We have designed a series of peptides that are highly specific for the extracellular domain of EGFR, based on our earlier studies on linear peptides. The previously reported linear peptide LARLLT, known to bind to EGFR, was modified with the goals of increasing its stability and its specificity toward EGFR. Peptide modifications, including D-amino acid substitution, cyclization, and chain reversal, were investigated. In addition, to facilitate labeling of the peptide with a fluorescent dye, an additional lysine residue was introduced onto the linear (KLARLLT) and cyclic peptides cyclo(KLARLLT) (Cyclo.L1). The lysine residue was also converted into an azide group in both a linear and reversed cyclic peptide sequences cyclo(K(N3)larllt) (Cyclo.L1.1) to allow for subsequent "click" conjugation. The cyclic peptides showed enhanced binding to EGFR by SPR. NMR and molecular modeling studies suggest that the peptides acquire a β-turn structure in solution. In vitro stability studies in human serum show that the cyclic peptide is more stable than the linear peptide.

Indexed as

Binding SitesCell Line, TumorCell ProliferationDrug DesignDrug StabilityErbB ReceptorsHumansHydrogen BondingLigandsMolecular Docking SimulationOligopeptidesPeptides, CyclicProtein Structure, SecondaryStructure-Activity RelationshipSurface Plasmon ResonanceErbB Receptorsleucyl-alanyl-arginyl-leucyl-leucyl-threonineLigandsOligopeptidesPeptides, Cycliccolorectal cancercyclic peptideEGFR extracellular domainlinear peptidesurface plasmon resonance

Identifiers

PMID29052959
PMCPMC5775921
OpenAlexW2765385012

What OpenQuestion holds

Textmetadata
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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.