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dc.contributor.author
Benavidez, Tomás Enrique  
dc.contributor.author
Torrente, Daniel  
dc.contributor.author
Marucho, Marcelo  
dc.contributor.author
Garcia, Carlos D  
dc.date.available
2018-08-01T19:19:27Z  
dc.date.issued
2015-03  
dc.identifier.citation
Benavidez, Tomás Enrique; Torrente, Daniel; Marucho, Marcelo; Garcia, Carlos D; Adsorption of soft and hard proteins onto OTCEs under the influence of an external electric field; American Chemical Society; Langmuir; 31; 8; 3-2015; 2455-2462  
dc.identifier.issn
0743-7463  
dc.identifier.uri
http://hdl.handle.net/11336/53811  
dc.description.abstract
The adsorption behavior of hard and soft proteins under the effect of an external electric field was investigated by a combination of spectroscopic ellipsometry and molecular dynamics (MD) simulations. Optically transparent carbon electrodes (OTCE) were used as conductive, sorbent substrates. Lysozyme (LSZ) and ribonuclease A (RNase A) were selected as representative hard proteins, whereas myoglobin (Mb), α-lactalbumin (α-LAC), bovine serum albumin (BSA), glucose oxidase (GOx), and immunoglobulin G (IgG) were selected to represent soft proteins. In line with recent publications from our group, the experimental results revealed that while the adsorption of all investigated proteins can be enhanced by the potential applied to the electrode, the effect is more pronounced for hard proteins. In contrast with the incomplete monolayers formed at open-circuit potential, the application of +800 mV to the sorbent surface induced the formation of multiple layers of protein. These results suggest that this effect can be related to the intrinsic polarizability of the protein (induction of dipoles), the resulting surface accessible solvent area (SASA), and structural rearrangements induced upon the incorporation on the protein layer. The described experiments are critical to understand the relationship between the structure of proteins and their tendency to form (under electric stimulation) layers with thicknesses that greatly surpass those obtained at open-circuit conditions.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
American Chemical Society  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Protein Adsorption  
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Soft Proteins  
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Hard Proteins  
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Otce  
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Otras Ciencias Químicas  
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Ciencias Químicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Adsorption of soft and hard proteins onto OTCEs under the influence of an external electric field  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2018-07-30T15:24:18Z  
dc.identifier.eissn
1520-5827  
dc.journal.volume
31  
dc.journal.number
8  
dc.journal.pagination
2455-2462  
dc.journal.pais
Estados Unidos  
dc.journal.ciudad
Washington DC  
dc.description.fil
Fil: Benavidez, Tomás Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina. University of Texas; Estados Unidos  
dc.description.fil
Fil: Torrente, Daniel. University of Texas; Estados Unidos  
dc.description.fil
Fil: Marucho, Marcelo. University of Texas; Estados Unidos  
dc.description.fil
Fil: Garcia, Carlos D. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina. University of Texas; Estados Unidos  
dc.journal.title
Langmuir  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/la504890v  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/la504890v  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4433030/