A pyrene-inhibitor fluorescent probe with large stokes shift for the staining of Aβ1–42, α-synuclein, and amylin amyloid fibrils as well as amyloid-containing staphylococcus aureus biofilms

Mahía, Alejandro; Conde-Giménez, María; Salillas, Sandra; Pallarés, Irantzu; Galano-Frutos, Juan J.; Lasa Uzcudun, Íñigo; Ventura, Salvador; Díaz-de-Villegas, María D.; Gálvez, José A.; Sancho, Javier

Publication:
A pyrene-inhibitor fluorescent probe with large stokes shift for the staining of Aβ1–42, α-synuclein, and amylin amyloid fibrils as well as amyloid-containing staphylococcus aureus biofilms

dc.contributor.author	Mahía, Alejandro
dc.contributor.author	Conde-Giménez, María
dc.contributor.author	Salillas, Sandra
dc.contributor.author	Pallarés, Irantzu
dc.contributor.author	Galano-Frutos, Juan J.
dc.contributor.author	Lasa Uzcudun, Íñigo
dc.contributor.author	Ventura, Salvador
dc.contributor.author	Díaz-de-Villegas, María D.
dc.contributor.author	Gálvez, José A.
dc.contributor.author	Sancho, Javier
dc.contributor.department	Ciencias de la Salud	es_ES
dc.contributor.department	Osasun Zientziak	eu
dc.date.accessioned	2021-12-09T12:25:21Z
dc.date.available	2021-12-09T12:25:21Z
dc.date.issued	2019
dc.description.abstract	Amyloid fibrils formed by a variety of peptides are biological markers of different human diseases, such as Alzheimer, Parkinson or Type II diabetes, and are structural constituents of bacterial biofilms. Novel fluorescent probes offering improved sensitivity or specificity towards that diversity of amyloid fibrils, or providing alternative spectral windows are needed to improve the detection or the identification of amyloid structures. One potential source for such new probes is offered by molecules known to interact with fibrils, such as the inhibitors of amyloid aggregation found in drug discovery projects. Here, we show the feasibility of the approach by designing, synthesizing and testing several pyrene-based fluorescent derivatives of a previously discovered inhibitor of the aggregation of the Aβ1-42 peptide. All the derivatives tested retain the interaction with the amyloid architecture and allow its staining. The more soluble derivative, compound 1D, stains similarly well amyloid fibrils formed by Aβ1-42, α-synuclein or amylin, provides a sensitivity only slightly lower than that of Thioflavin T, displays a large Stokes shift, allows an efficient excitation in the UV spectral region,and it is not cytotoxic. Compound 1D can also stain amyloid fibrils formed by Staphylococcal peptides present in biofilm matrices and can be used to distinguish, by direct staining,S. aureus biofilms containing amyloid forming phenol soluble modulins from those lacking them.	en
dc.description.sponsorship	IL is supported by the Spanish Ministry of Economy and Competitiveness grant BIO2014-53530-R. SVis supported by grant BIO2016-783-78310-R and by ICREA (ICREA Academia 2015). MDD is supported by the Government of Aragon (GA E-102). JS is supported by grants BFU2016-78232-P (MINECO, Spain) and E45_17R (Gobierno de Aragón, Spain). JS and IL acknowledge financial support from grant CI-2017/001-3 (Campus Iberus, Spain). AM was a recipient of a predoctoral FPU fellowship from the Spanish Government.	en
dc.format.extent	28 p.
dc.format.mimetype	application/pdf	en
dc.identifier.doi	10.1007/s00216-018-1433-8
dc.identifier.uri	https://academica-e.unavarra.es/handle/2454/41220
dc.language.iso	eng	en
dc.publisher	Springer	en
dc.relation.ispartof	Analytical and Bioanalytical Chemistry (2019) 411:251–265	en
dc.relation.projectID	info:eu-repo/grantAgreement/MINECO//BIO2014-53530-R/ES/	en
dc.relation.projectID	info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BIO2017-83035-R/ES/	en
dc.relation.projectID	info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2016-78232-P	en
dc.relation.publisherversion	https://doi.org/10.1007/s00216-018-1433-8
dc.rights	© Springer-Verlag GmbH Germany, part of Springer Nature 2018	en
dc.rights.accessRights	info:eu-repo/semantics/openAccess	en
dc.rights.accessRights	Acceso abierto / Sarbide irekia	es
dc.subject	Amyloid fibrils	en
dc.subject	Aggregation inhibitor	en
dc.subject	Pyrene	en
dc.subject	Stokes shift	en
dc.subject	Fluorescent probes	en
dc.subject	Biofilm matrix	en
dc.title	A pyrene-inhibitor fluorescent probe with large stokes shift for the staining of Aβ1–42, α-synuclein, and amylin amyloid fibrils as well as amyloid-containing staphylococcus aureus biofilms	en
dc.type	info:eu-repo/semantics/article
dc.type.version	info:eu-repo/semantics/acceptedVersion	en
dc.type.version	Versión aceptada / Onetsi den bertsioa	es
dspace.entity.type	Publication
relation.isAuthorOfPublication	c654d104-1ae2-41cf-9215-4b4bed3e5ea6
relation.isAuthorOfPublication.latestForDiscovery	c654d104-1ae2-41cf-9215-4b4bed3e5ea6