Web of Science: 4 citations, Scopus: 3 citations, Google Scholar: citations,
Design and characterization of high-affinity synthetic peptides as bioreceptors for diagnosis of cutaneous leishmaniasis
Prada, Y. A. (Universidad Industrial de Santander. Laboratorio de Espectroscopia Atómica y Molecular)
Soler Aznar, Maria (Institut Català de Nanociència i Nanotecnologia)
Guzmán, Fanny (Pontificia Universidad Católica de Valparaíso. Laboratorio de Síntesis de Péptidos)
Castillo, John J. (Universidad Industrial de Santander. Grupo de Investigación en Bioquímica y Microbiología)
Lechuga, Laura M (Institut Català de Nanociència i Nanotecnologia)
Mejía-Ospino, Enrique (Universidad Industrial de Santander. Laboratorio de Espectroscopia Atómica y Molecular)

Date: 2021
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 KD are in the nanomolar range, which is comparable to high-affinity antibodies, with the additional advantage of a high biochemical stability and simpler production. Pep2854 exhibited a high affinity for sAP (KD = 1. 48 nM) while Pep2856 had a good affinity for PPG (KD 1. 76 nM). This study evidences that these peptidomimetics represent a novel alternative tool to the use of high molecular weight proteins for biorecognition in the diagnostic test and biosensor devices for CL.
Grants: Ministerio de Ciencia e Innovación SEV-2017-0706
Ministerio de Ciencia e Innovación FICTS-1420-27
Rights: Tots els drets reservats.
Language: Anglès
Document: Article ; recerca ; Versió acceptada per publicar
Subject: Cutaneous leishmaniasis ; High-affinity peptides ; Lectins ; Proteophosphoglycans ; Acid phosphatase
Published in: Analytical and bioanalytical chemistry, Vol. 413, issue 17 (July 2021) , p. 4545-4555, ISSN 1618-2650

DOI: 10.1007/s00216-021-03424-2
PMID: 34037808


Postprint
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The record appears in these collections:
Research literature > UAB research groups literature > Research Centres and Groups (research output) > Experimental sciences > Catalan Institute of Nanoscience and Nanotechnology (ICN2)
Articles > Research articles
Articles > Published articles

 Record created 2021-07-28, last modified 2023-11-05



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