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dc.contributor.author
Ledesma, Ana Estela
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Chemes, Doly María
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Frías, María de los Ángeles
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Guauque Torres, María del Pilar
dc.date.available
2019-02-06T17:29:06Z
dc.date.issued
2017-08
dc.identifier.citation
Ledesma, Ana Estela; Chemes, Doly María; Frías, María de los Ángeles; Guauque Torres, María del Pilar; Spectroscopic characterization and docking studies of ZnO nanoparticle modified with BSA; Elsevier Science; Applied Surface Science; 412; 8-2017; 177-188
dc.identifier.issn
0169-4332
dc.identifier.uri
http://hdl.handle.net/11336/69519
dc.description.abstract
Nanoparticles (NP) into a biological environment are an interesting topic for diagnosis and therapy in applications for medicine or environment and the knowledge about this interaction is important from the perspective of safe use of nanomaterials. In the current study, we characterized the type of interaction and the orientation of bovine serum albumin (BSA) adsorbed on ZnO nanoparticle surfaces as a function of size, using molecular docking. To probe experimentally different theoretical hypothesis about the interaction, ZnO-NPs were prepared in aqueous solution, and then were bioconjugated with BSA. Transmission electron microscopy (TEM) and Raman spectroscopy confirm the spherical shape of NP and the irreversible adsorption of BSA on NP surface. Raman and Infrared spectroscopy (FTIR) reveal that BSA interaction with ZnO nanoparticle produced a conformational rearrangement into protein, observing changes in Tyr and Trp environment, a minor percentage of α-helix structure and a more extended chain. The fluorescence analysis demonstrated that when BSA concentration higher than 30 μM is used the signal due to the self-oligomerization of protein overlaps with the ZnO nanoparticle emission. The results predicted that the most probable interaction site is near to domain IB and IIA and ionic interactions are the major responsible for the binding. Thermal stability studies reveals that the denaturalization temperature of BSA increase from 57 °C to 65 °C in presence of ZnO NP and their esterase-like activity was improved.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Bsa Protein
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Esterase-Like Activity
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Ftir And Raman Spectroscopic
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Molecular Docking
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Thermal Stability
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Zno Nanoparticles
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Otras Ciencias Químicas
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Spectroscopic characterization and docking studies of ZnO nanoparticle modified with BSA
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-01-14T16:29:23Z
dc.journal.volume
412
dc.journal.pagination
177-188
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Ledesma, Ana Estela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
dc.description.fil
Fil: Chemes, Doly María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Química del Noroeste. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia. Instituto de Química del Noroeste; Argentina
dc.description.fil
Fil: Frías, María de los Ángeles. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
dc.description.fil
Fil: Guauque Torres, María del Pilar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
dc.journal.title
Applied Surface Science
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1016/j.apsusc.2017.03.202
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0169433217308942
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