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Serum-PEG and BSA-PEG hydrogels as advanced platforms for evaluating plasma protein binding

2025-04Artigo científico Acesso aberto
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datacite.subject.fosCiências Médicas::Ciências da Saúde
datacite.subject.fosCiências Naturais::Ciências Químicas
datacite.subject.fosEngenharia e Tecnologia::Engenharia dos Materiais
datacite.subject.sdg03:Saúde de Qualidade
datacite.subject.sdg09:Indústria, Inovação e Infraestruturas
dc.contributor.authorCoelho, Carlos D.F.
dc.contributor.authorPaiva, Victor S.
dc.contributor.authorAlmeida, Zaida L.
dc.contributor.authorJesus, João A.
dc.contributor.authorMarteleira, Madalena
dc.contributor.authorRamos, Cristiana V.
dc.contributor.authorCruz, Pedro F.
dc.contributor.authorCosta, Telma
dc.contributor.authorMoura, Carla S.
dc.contributor.authorTrindade, Daniela
dc.contributor.authorBrito, Rui M.M.
dc.contributor.authorLagoa, Ricardo
dc.contributor.authorVaz, Daniela C.
dc.contributor.authorMoreno, Maria João
dc.date.accessioned2026-10-02T15:11:53Z
dc.date.available2026-10-02T15:11:53Z
dc.date.issued2025-04
dc.descriptionArticle number: 102565.
dc.descriptionAcknowledgment: The authors acknowledge the Rede Nacional de Ressonância Magnética Nuclear (RNRMN, UC-NMR) for access to the NMR equipment, and Sérgio Seixas de Melo (from CQC-IMS) for access to the photoluminescence equipment including the confocal FLIM system and the absolute photoluminescence quantum yield spectrometer.
dc.description.abstractThe binding of bioactive compounds to proteins is critical for their availability and ADME/Tox profile. Specifically, binding to serum proteins affects both the distribution and elimination of drugs, while permeation through protein-enriched matrices, such as skin, is also influenced by protein interactions. Although several methods exist to evaluate ligand-protein binding, they often fail to replicate the high protein concentrations and molecular crowding conditions found in vivo. In this study, we investigate the use of protein-PEG hydrogels with low crosslinking density as 3D matrices to quantify ligand-protein affinity. Two types of hydrogels were developed: one using bovine serum albumin (BSA) and a more physiologically relevant one using serum. BSA was chosen as a model protein due to its similarity to human serum albumin. The hydrogels were characterized for swelling, stability, mechanical properties, and porosity, and the structural integrity of BSA within the hydrogel was confirmed using circular dichroism, 1H NMR and fluorescence spectroscopy. To assess protein functionality, we evaluated the binding affinity of various ligands, including a homologous series of fluorescent amphiphiles with different hydrophobicity (NBD-Cn, where n = 4, 6, and 8), two pesticides (malathion and chlorpyrifos), and six pharmaceutical drugs (acetaminophen, chlorpromazine, diclofenac, labetalol, salicylic acid, and verapamil). Our results demonstrated that the structural and functional properties of BSA remained intact within the hydrogel, and the large mesh size allowed for rapid and selective ligand binding. A comparison of BSA and serum hydrogels confirmed the major role of serum albumin in ligand binding, while highlighting some differences between cationic and anionic ligands. Altogether, these hydrogels offer an effective and reliable 3D platform for the fast and accurate evaluation of plasma protein binding of drugs and other bioactive compounds.eng
dc.description.sponsorshipFunding sources: This research was funded by the European Regional Development Fund, through the COMPETE2020-Operational Program for Competitiveness and Internationalization, and Portuguese funds via FCT-Fundação para a Ciência e a Tecnologia, under projects UIDB/00313/2020, UIDP/00313/2020, and PTDC/BIA-MIB/31864/2017 (Portugal).
dc.identifier.citationCoelho, C. D. F., Paiva, V. S., Almeida, Z. L., Jesus, J. A., Marteleira, M., Ramos, C. V., Cruz, P. F., Costa, T., Moura, C. S., Trindade, D., Brito, R. M. M., Lagoa, R., Vaz, D. C., & Moreno, M. J. (2025). Serum-PEG and BSA-PEG hydrogels as advanced platforms for evaluating plasma protein binding. Materials Today Chemistry, 45, Artigo 102565, 1–14. https://doi.org/10.1016/j.mtchem.2025.102565
dc.identifier.doi10.1016/j.mtchem.2025.102565
dc.identifier.issn2468-5194
dc.identifier.urihttp://hdl.handle.net/10400.8/16957
dc.language.isoeng
dc.peerreviewedyes
dc.publisherElsevier
dc.relationCoimbra Chemistry Center
dc.relationCoimbra Chemistry Center
dc.relationMultifunctional biomolecular systems for new methods of decontamination, protection and toxicological assessment
dc.relation.hasversionhttps://doi.org/10.1016/j.mtchem.2025.102565
dc.relation.ispartofMaterials Today Chemistry
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectADME/Tox profile
dc.subjectBioassay
dc.subjectBiomaterial
dc.subjectBlood serum
dc.subjectLarge-mesh hydrogels
dc.subjectLigand-protein binding
dc.subjectPharmacokinetics
dc.subjectSerum albumin
dc.titleSerum-PEG and BSA-PEG hydrogels as advanced platforms for evaluating plasma protein bindingeng
dc.typejournal article
dspace.entity.typePublication
oaire.awardNumberUIDB/00313/2020
oaire.awardNumberUIDP/00313/2020
oaire.awardNumberPTDC/BIA-MIB/31864/2017
oaire.awardTitleCoimbra Chemistry Center
oaire.awardTitleCoimbra Chemistry Center
oaire.awardTitleMultifunctional biomolecular systems for new methods of decontamination, protection and toxicological assessment
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F00313%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP%2F00313%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-MIB%2F31864%2F2017/PT
oaire.citation.endPage14
oaire.citation.startPage1
oaire.citation.titleMaterials Today Chemistry
oaire.citation.volume45
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream3599-PPCDT
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85
person.familyNameFigueira Coelho
person.familyNameMonteiro de Moura
person.familyNameTrindade
person.familyNameLagoa
person.familyNameBarroso de Moura Cipreste Vaz
person.givenNameCarlos Daniel
person.givenNameCarla Sofia
person.givenNameDaniela Alexandra
person.givenNameRicardo
person.givenNameDaniela
person.identifier124357
person.identifier.ciencia-id671C-8FEC-A14A
person.identifier.ciencia-id6316-1507-A39A
person.identifier.ciencia-id5C18-A29A-44AB
person.identifier.ciencia-id801A-7761-328C
person.identifier.orcid0000-0002-0975-9545
person.identifier.orcid0000-0003-2610-1005
person.identifier.orcid0000-0003-3621-7095
person.identifier.orcid0000-0003-2375-6612
person.identifier.orcid0000-0001-7562-4676
person.identifier.ridR-5243-2017
person.identifier.scopus-author-id23051352300
person.identifier.scopus-author-id6602838931
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
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