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dc.contributor.authorPuiggalí Jou, Anna
dc.contributor.authorValle Mendoza, Luis Javier del
dc.contributor.authorAlemán Llansó, Carlos
dc.contributor.authorPérez Madrigal, Mª del Mar
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament d'Enginyeria Química
dc.date.accessioned2017-05-10T11:35:48Z
dc.date.available2017-11-14T01:30:36Z
dc.date.issued2017-02-01
dc.identifier.citationPuiggali, A., del Valle, LJ., Aleman, C., Pérez-Madrigal, M. M. Weighing biointeractions between fibrin (ogen) and clot-binding peptides using microcantilever sensors. "Journal of peptide science", 1 Febrer 2017, vol. 23, núm. 2, p. 162-171.
dc.identifier.issn1075-2617
dc.identifier.urihttp://hdl.handle.net/2117/104268
dc.descriptionThis is the peer reviewed version of the following article: “Puiggalí, A., Del Valle, L.J., Aleman, C. and Pérez, M. (2017) Weighing biointeractions between fibrin (ogen) and clot-binding peptides using microcantilever sensors. Journal of peptide science, (23) 2: 162–171.” which has been published in final form at [doi: 10.1002/psc.2938]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving."
dc.description.abstractPeptides homing tumor vasculature are considered promising molecular imaging agents for cancer detection at an early stage. In addition to their high binding affinity, improved tissue penetrating ability, and low immunogenicity, they can deliver targeted anticancer drugs, thus expanding therapeutic treatments. Among those, CREKA, a linear peptide that specifically binds to clotted-plasma proteins in tumor vessels, has been recently employed to design bioactive systems able to target different cancer types. Within this context, this paper explores the biorecognition event between CR(NMe)EKA, an engineered CREKA-analog bearing a noncoded amino acid (N-methyl-Glu) that is responsible for its enhanced activity, and clotted-plasma proteins (fibrin and fibrinogen) by nanomechanical detection. Specifically, the tumor-homing peptide was covalently attached via epoxysilane chemistry onto silicon microcantilever chips that acted as sensors during dynamic mode experiments. Before that, each step of the functionalization process was followed by contact angle measurements, interferometry, X-ray photoelectron spectroscopy, and atomic force microscopy, thus revealing the applied protocol as a suitable strategy. The fibrin(ogen)-binding induced by CR(NMe)EKA was detected by the resonance frequency shift of the cantilevers, and a detection limit of 100¿ng/mL was achieved for both proteins. Even though further development is required, this work reflects the promising application of emerging technologies capable of assisting in the comprehension of biological interactions and their implications in the biotechnological field.
dc.format.extent10 p.
dc.language.isoeng
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Spain
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.subjectÀrees temàtiques de la UPC::Enginyeria química
dc.subject.lcshPeptides
dc.subject.lcshPolymers in medicine
dc.subject.lcshCancer--Treatment
dc.subject.otherfibrin
dc.subject.otherfibrinogen
dc.subject.otherprotein binding
dc.subject.othertumor-homing peptide
dc.subject.otherCys-Arg-Glu-Lys-Ala (CREKA)
dc.subject.othernanomechanical sensing
dc.subject.othermicrocantilevers
dc.titleWeighing biointeractions between fibrin (ogen) and clot-binding peptides using microcantilever sensors
dc.typeArticle
dc.subject.lemacPèptids
dc.subject.lemacCàncer -- Tractament
dc.contributor.groupUniversitat Politècnica de Catalunya. PSEP - Polimers Sintètics: Estructura i Propietats. Polimers Biodegradables
dc.contributor.groupUniversitat Politècnica de Catalunya. IMEM - Innovació, Modelització i Enginyeria en (BIO) Materials
dc.identifier.doi10.1002/psc.2938
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://onlinelibrary.wiley.com/doi/10.1002/psc.2938/abstract
dc.rights.accessOpen Access
local.identifier.drac20096782
dc.description.versionPostprint (author's final draft)
local.citation.authorPuiggali, A.; del Valle, LJ.; Aleman, C.; Pérez-Madrigal, Maria M.
local.citation.publicationNameJournal of peptide science
local.citation.volume23
local.citation.number2
local.citation.startingPage162
local.citation.endingPage171


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