A new class of sensing elements for sensors: Clamp peptides for Zika virus.

Antibody mimetics Binding assay Clamp peptides Computational methods Dengue virus Label-free impedance sensors Molecular modelling Zika virus

Journal

Biosensors & bioelectronics
ISSN: 1873-4235
Titre abrégé: Biosens Bioelectron
Pays: England
ID NLM: 9001289

Informations de publication

Date de publication:
01 Nov 2021
Historique:
received: 20 02 2021
revised: 25 05 2021
accepted: 28 06 2021
pubmed: 11 7 2021
medline: 20 8 2021
entrez: 10 7 2021
Statut: ppublish

Résumé

The design of a new class of selective and high affinity antibody mimetics termed clamp peptide (CP) that incorporate three short peptides structurally and mechanically mimicking a clamp is proposed as sensing elements for a reliable detection sensor platform. The CPs consist of two short peptides functioning as arms that recognize two different epitopes in the target protein and are connected by a third short peptide that acts as a hinge between the peptide arms. For the construction of CPs, we employed a rational design combined with computational methods. To illustrate our approach, we designed a CP that binds selectively to the envelope protein of the Zika virus (ZIKV). The virtual docking cycles were run maximizing the discrimination between ZIKV and Dengue virus (DENV) envelope proteins. DENV was chosen among the flavivirus family because it has high structural similarity with ZIKV. When employed in a colorimetric binding assay or in label-free electrochemical impedance sensor format, the CP was selective for ZIKV vs DENV particles showing detection limit under 10

Identifiants

pubmed: 34246123
pii: S0956-5663(21)00508-X
doi: 10.1016/j.bios.2021.113471
pii:
doi:

Substances chimiques

Antibodies, Viral 0
Peptides 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

113471

Informations de copyright

Copyright © 2021. Published by Elsevier B.V.

Auteurs

Marcello Mascini (M)

Faculty of Bioscience and Technology for Food, Agriculture and Environment, University of Teramo, 64100, Teramo, Italy; Department of Analytical Chemistry, Faculty of Chemistry, University Complutense of Madrid, Ciudad Universitaria S/n, 28040, Madrid, Spain. Electronic address: mmascini@unite.it.

Emre Dikici (E)

Department of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL, 33136, United States; Dr. JT Macdonald Foundation Biomedical Nanotechnology Institute, University of Miami, Miami, FL, 33136, United States.

Julio A Perez-Erviti (JA)

Center for Protein Studies, Faculty of Biology, University of Havana, La Havana, 10400, Cuba.

Sapna K Deo (SK)

Department of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL, 33136, United States; Dr. JT Macdonald Foundation Biomedical Nanotechnology Institute, University of Miami, Miami, FL, 33136, United States.

Dario Compagnone (D)

Faculty of Bioscience and Technology for Food, Agriculture and Environment, University of Teramo, 64100, Teramo, Italy.

Sylvia Daunert (S)

Department of Biochemistry and Molecular Biology, Miller School of Medicine, University of Miami, Miami, FL, 33136, United States; Dr. JT Macdonald Foundation Biomedical Nanotechnology Institute, University of Miami, Miami, FL, 33136, United States; University of Miami Clinical and Translational Science Institute, University of Miami, Miami, FL, 33136, United States. Electronic address: sdaunert@med.miami.edu.

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Classifications MeSH