Evidence map›Paper›PMID 34037808›Full record

ArticleAnalytical and bioanalytical chemistry2021

Design and characterization of high-affinity synthetic peptides as bioreceptors for diagnosis of cutaneous leishmaniasis.

Y Andrea Prada, Maria Soler, Fanny Guzmán, John J Castillo, Laura M Lechuga, Enrique Mejía-Ospino

Open access · bronzeAbstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.4field-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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
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

6 authors at 3 institutions in 3 countries.

Y Andrea PradaLaboratorio de Espectroscopia Atómica y Molecular (LEAM), Universidad Industrial de Santander, Carrera 27 Calle 9, Bucaramanga, Santander, 678, Colombia.
Maria SolerNetworking Research Center on Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), 28029, Madrid, Spain.
Fanny GuzmánLaboratorio de Síntesis de Péptidos, Núcleo de Biotecnología Curauma (NBC), Pontificia Universidad Católica de Valparaíso, 2373223, Valparaíso, Chile.
John J CastilloGrupo de Investigación en Bioquímica y Microbiología (GIBIM), Universidad Industrial de Santander, Bucaramanga, 680002, Colombia. jcasleon@uis.edu.co.
Laura M LechugaNetworking Research Center on Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), 28029, Madrid, Spain.
Enrique Mejía-OspinoLaboratorio de Espectroscopia Atómica y Molecular (LEAM), Universidad Industrial de Santander, Carrera 27 Calle 9, Bucaramanga, Santander, 678, Colombia.
Industrial University of Santander · COBiomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine · ESPontificia Universidad Católica de Valparaíso · CL

Funding

CERCA programme/Generalitat de Catalunya SEV-2017-0706
6 · The paper itself

Abstract

Cutaneous leishmaniasis (CL) is one of the illnesses caused by Leishmania parasite infection, which can be asymptomatic or severe according to the infecting Leishmania strain. CL is commonly diagnosed by directly detecting the parasites or their DNA in tissue samples. New diagnostic methodologies target specific proteins (biomarkers) secreted by the parasite during the infection process. However, specific bioreceptors for the in vivo or in vitro detection of these novel biomarkers are rather limited in terms of sensitivity and specificity. For this reason, we here introduce three novel peptides as bioreceptors for the highly sensitive and selective identification of acid phosphatase (sAP) and proteophosphoglycan (PPG), which have a crucial role in leishmaniasis infection. These high-affinity peptides have been designed from the conservative domains of the lectin family, holding the ability to interact with the biological target and produce the same effect than the original protein. The synthetic peptides have been characterized and the affinity and kinetic constants for their interaction with the targets (sAP and PPG) have been determined by a surface plasmon resonance biosensor. Values obtained for K

Indexed as

Acid PhosphataseBinding SitesHumansLeishmaniaLeishmaniasis, CutaneousMembrane ProteinsModels, MolecularPeptidesPeptidomimeticsProteoglycansProtozoan ProteinsSurface Plasmon ResonanceAcid PhosphataseMembrane ProteinsPeptidesPeptidomimeticsPpg1 protein, LeishmaniaProteoglycansProtozoan ProteinsAcid phosphataseCutaneous leishmaniasisHigh-affinity peptidesLectinsProteophosphoglycans

Identifiers

PMID34037808
PMCPMC8149292
OpenAlexW3165471871

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.