Fluorometric Measurement of Calmodulin-Dependent Peptide–Protein Interactions Using Dansylated Calmodulin

© 2024 The Authors; exclusive licensee Bio-protocol LLC. This is an open access article under the CC BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).

Detalles Bibliográficos
Autores: Núñez, Eider, Muguruza-Montero, Arantza, Alicante Martínez, Sara, Villarroel, Álvaro
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2024
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/362282
Acceso en línea:http://hdl.handle.net/10261/362282
Access Level:acceso abierto
Palabra clave:Dansyl-Calmodulin
CaM-target
Steady-state fluorescence spectroscopy
Calcium dependency
Dansylchloride
Peptide
Protein
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spelling Fluorometric Measurement of Calmodulin-Dependent Peptide–Protein Interactions Using Dansylated CalmodulinNúñez, EiderMuguruza-Montero, ArantzaAlicante Martínez, SaraVillarroel, ÁlvaroDansyl-CalmodulinCaM-targetSteady-state fluorescence spectroscopyCalcium dependencyDansylchloridePeptideProtein© 2024 The Authors; exclusive licensee Bio-protocol LLC. This is an open access article under the CC BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).The assessment of peptide–protein interactions is a pivotal aspect of studying the functionality and mechanisms of various bioactive peptides. In this context, it is essential to employ methods that meet specific criteria, including sensitivity, biocompatibility, versatility, simplicity, and the ability to offer real-time monitoring. In cellular contexts, only a few proteins naturally possess inherent fluorescence, specifically those containing aromatic amino acids, particularly tryptophan. Nonetheless, by covalently attaching fluorescent markers, almost all proteins can be modified for monitoring purposes. Among the early extrinsic fluorescent probes designed for this task, dansyl chloride (DNSC) is a notable option due to its versatile nature and reliable performance. DNSC has been the primary choice as a fluorogenic derivatizing reagent for analyzing amino acids in proteins and peptides for an extended period of time. In our work, we have effectively utilized the distinctive properties of dansylated-calmodulin (D-CaM) for monitoring the interaction dynamics between proteins and peptides, particularly in the context of their association with calmodulin (CaM), a calcium-dependent regulatory protein. This technique not only enables us to scrutinize the affinity of diverse ligands but also sheds light on the intricate role played by calcium in these interactions.This article has been funded through the following research projects: the Ministry of Science and Innovation under the project PID2021-128286NB-100 funded by MCIN/AEI/10.13039/501100011033/FEDER, UE; support from the Basque Government under the project IT1707-22. S.M-A and E.N. received support from predoctoral (PRE_2021_1_0101) and postdoctoral (POS_2021_1_0017) contracts, respectively, provided by the Basque GovernmentPeer reviewedBio-protocol LLCMinisterio de Ciencia e Innovación (España)Agencia Estatal de Investigación (España)Eusko JaurlaritzaNúñez, Eider [0000-0001-8075-9815]Muguruza-Montero, Arantza [0000-0001-8713-4949]Villarroel, Álvaro [0000-0003-1096-7824]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202420242024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/362282reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-128286NB-I00https://doi.org/10.21769/BioProtoc.4963Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3622822026-05-22T06:33:51Z
dc.title.none.fl_str_mv Fluorometric Measurement of Calmodulin-Dependent Peptide–Protein Interactions Using Dansylated Calmodulin
title Fluorometric Measurement of Calmodulin-Dependent Peptide–Protein Interactions Using Dansylated Calmodulin
spellingShingle Fluorometric Measurement of Calmodulin-Dependent Peptide–Protein Interactions Using Dansylated Calmodulin
Núñez, Eider
Dansyl-Calmodulin
CaM-target
Steady-state fluorescence spectroscopy
Calcium dependency
Dansylchloride
Peptide
Protein
title_short Fluorometric Measurement of Calmodulin-Dependent Peptide–Protein Interactions Using Dansylated Calmodulin
title_full Fluorometric Measurement of Calmodulin-Dependent Peptide–Protein Interactions Using Dansylated Calmodulin
title_fullStr Fluorometric Measurement of Calmodulin-Dependent Peptide–Protein Interactions Using Dansylated Calmodulin
title_full_unstemmed Fluorometric Measurement of Calmodulin-Dependent Peptide–Protein Interactions Using Dansylated Calmodulin
title_sort Fluorometric Measurement of Calmodulin-Dependent Peptide–Protein Interactions Using Dansylated Calmodulin
dc.creator.none.fl_str_mv Núñez, Eider
Muguruza-Montero, Arantza
Alicante Martínez, Sara
Villarroel, Álvaro
author Núñez, Eider
author_facet Núñez, Eider
Muguruza-Montero, Arantza
Alicante Martínez, Sara
Villarroel, Álvaro
author_role author
author2 Muguruza-Montero, Arantza
Alicante Martínez, Sara
Villarroel, Álvaro
author2_role author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia e Innovación (España)
Agencia Estatal de Investigación (España)
Eusko Jaurlaritza
Núñez, Eider [0000-0001-8075-9815]
Muguruza-Montero, Arantza [0000-0001-8713-4949]
Villarroel, Álvaro [0000-0003-1096-7824]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Dansyl-Calmodulin
CaM-target
Steady-state fluorescence spectroscopy
Calcium dependency
Dansylchloride
Peptide
Protein
topic Dansyl-Calmodulin
CaM-target
Steady-state fluorescence spectroscopy
Calcium dependency
Dansylchloride
Peptide
Protein
description © 2024 The Authors; exclusive licensee Bio-protocol LLC. This is an open access article under the CC BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
publishDate 2024
dc.date.none.fl_str_mv 2024
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/362282
url http://hdl.handle.net/10261/362282
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2021-128286NB-I00
https://doi.org/10.21769/BioProtoc.4963
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Bio-protocol LLC
publisher.none.fl_str_mv Bio-protocol LLC
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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