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dc.contributor.authorGonzález Posada, Alexa Hibet-
dc.contributor.authorMesa Cadavid, Mónica-
dc.contributor.authorSierra García, Ligia-
dc.contributor.authorLópez Osorio, Betty Lucy-
dc.date.accessioned2024-09-24T14:34:12Z-
dc.date.available2024-09-24T14:34:12Z-
dc.date.issued2024-
dc.identifier.citationA. H. Gonzalez-Posada, M. Mesa, L. Sierra & B. Lopez (13 Sep 2024): Interactions of human serum albumin with phosphate and Tris buffers: impact on paclitaxel binding and nanoparticles self-assembly, Journal of Microencapsulation, DOI: 10.1080/02652048.2024.2389135spa
dc.identifier.issn0265-2048-
dc.identifier.urihttps://hdl.handle.net/10495/42372-
dc.description.abstractABSTRACT: Aim: To investigate the conformational changes in human serum albumin (HSA) caused by chemical (CD) and thermal denaturation (TD) at pH 7.4 and 9.9, crucial for designing controlled drug delivery systems with paclitaxel (PTX). Methods: Experimental and computational methods, including differential scanning calorimetry (DSC), UV-Vis and intrinsic fluorescence spectroscopy, mean diameter, polydispersity index (PDI), ζ-potential, encapsulation efficiency (EE), in vitro release and protein docking studies were conducted to study the HSA denaturation and nanoparticles (NPs) preparation. Results: TD at pH 7.4 produced smaller NPs (287.1±12.9nm) than CD at pH 7.4 with NPs (584.2±47.7nm). TD at pH 9.9 exhibited high EE (97.3±0.2%w/w) with rapid PTX release (50% within 1h), whereas at pH 7.4 (96.4±2.1%w/w), release only 40%. ζ-potentials were around −30mV. Conclusion: Buffer type and pH significantly influence NP properties. TD in PBS at pH 7.4, provided optimal conditions for a stable and efficient drug delivery system.spa
dc.format.extent13 páginasspa
dc.format.mimetypeapplication/pdfspa
dc.language.isoengspa
dc.publisherTaylor and Francisspa
dc.type.hasversioninfo:eu-repo/semantics/publishedVersionspa
dc.rightsinfo:eu-repo/semantics/openAccessspa
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/2.5/co/*
dc.titleInteractions of human serum albumin with phosphate and Tris buffers: impact on paclitaxel binding and nanoparticles self-assemblyspa
dc.typeinfo:eu-repo/semantics/articlespa
dc.publisher.groupCiencia de los Materialesspa
dc.identifier.doi10.1080/02652048.2024.2389135-
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85spa
dc.rights.accessrightshttp://purl.org/coar/access_right/c_abf2spa
dc.identifier.eissn1464-5246-
oaire.citationtitleJournal of Microencapsulationspa
oaire.citationstartpage1spa
oaire.citationendpage13spa
dc.rights.creativecommonshttps://creativecommons.org/licenses/by-nc-nd/4.0/spa
oaire.fundernameColombia. Ministerio de Ciencia, Tecnología e Innovación - MinCienciasspa
dc.publisher.placeLondres, Inglaterraspa
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1spa
dc.type.redcolhttps://purl.org/redcol/resource_type/ARTspa
dc.type.localArtículo de investigaciónspa
dc.subject.decsAlbúmina Sérica Humana-
dc.subject.decsSerum Albumin, Human-
dc.subject.decsDesnaturalización Proteica-
dc.subject.decsProtein Denaturation-
dc.subject.decsPaclitaxel Unido a Albúmina-
dc.subject.decsAlbumin-Bound Paclitaxel-
dc.subject.decsPaclitaxel-
dc.description.researchgroupidCOL0002401spa
oaire.awardnumberMinCiencias Convocatoria 785 de 2017spa
dc.subject.meshurihttps://id.nlm.nih.gov/mesh/D000075462-
dc.subject.meshurihttps://id.nlm.nih.gov/mesh/D011489-
dc.subject.meshurihttps://id.nlm.nih.gov/mesh/D000068196-
dc.subject.meshurihttps://id.nlm.nih.gov/mesh/D017239-
dc.relation.ispartofjournalabbrevJ. Microencapsul.spa
oaire.funderidentifier.rorRoR:03fd5ne08-
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